{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O87778","uniProtkbId":"DNAJ_LATSK","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-11-01","entryVersion":127,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Chaperone protein DnaJ"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"dnaJ"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Binds 2 Zn(2+) ions per monomer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"value":"By heat shock as well as salt or ethanol stress"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"value":"Belongs to the DnaJ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Chaperone protein DnaJ","featureId":"PRO_0000070805"},{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"J","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Repeat","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"CXXCXGXG motif"},{"type":"Repeat","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"CXXCXGXG motif"},{"type":"Repeat","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"CXXCXGXG motif"},{"type":"Repeat","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"CXXCXGXG motif"},{"type":"Zinc finger","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"CR-type","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}]},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01152"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}}],"keywords":[{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0677","category":"Domain","name":"Repeat"},{"id":"KW-0346","category":"Biological process","name":"Stress response"},{"id":"KW-0862","category":"Ligand","name":"Zinc"},{"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"10553284","citationType":"journal article","authors":["Schmidt G.","Hertel C.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"10553284"},{"database":"DOI","id":"10.1016/s0723-2020(99)80039-3"}],"title":"Molecular characterisation of the dnaK operon of Lactobacillus sakei LTH681.","publicationDate":"1999","journal":"Syst. Appl. Microbiol.","firstPage":"321","lastPage":"328","volume":"22"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH681","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006274","properties":[{"key":"ProteinId","value":"CAA06942.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_016265324.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP017931.1"}]},{"database":"AlphaFoldDB","id":"O87778","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O87778","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0031072","properties":[{"key":"GoTerm","value":"F:heat shock protein binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042026","properties":[{"key":"GoTerm","value":"P:protein refolding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009408","properties":[{"key":"GoTerm","value":"P:response to heat"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06257","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd10747","properties":[{"key":"EntryName","value":"DnaJ_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd10719","properties":[{"key":"EntryName","value":"DnaJ_zf"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.110:FF:000031","properties":[{"key":"EntryName","value":"Molecular chaperone DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.10.230.10:FF:000002","properties":[{"key":"EntryName","value":"Molecular chaperone DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.260.20:FF:000004","properties":[{"key":"EntryName","value":"Molecular chaperone DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.110","properties":[{"key":"EntryName","value":"DnaJ domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.10.230.10","properties":[{"key":"EntryName","value":"Heat shock protein DnaJ, cysteine-rich domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.260.20","properties":[{"key":"EntryName","value":"Urease metallochaperone UreE, N-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01152","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012724","properties":[{"key":"EntryName","value":"DnaJ"}]},{"database":"InterPro","id":"IPR002939","properties":[{"key":"EntryName","value":"DnaJ_C"}]},{"database":"InterPro","id":"IPR001623","properties":[{"key":"EntryName","value":"DnaJ_domain"}]},{"database":"InterPro","id":"IPR018253","properties":[{"key":"EntryName","value":"DnaJ_domain_CS"}]},{"database":"InterPro","id":"IPR008971","properties":[{"key":"EntryName","value":"HSP40/DnaJ_pept-bd"}]},{"database":"InterPro","id":"IPR001305","properties":[{"key":"EntryName","value":"HSP_DnaJ_Cys-rich_dom"}]},{"database":"InterPro","id":"IPR036410","properties":[{"key":"EntryName","value":"HSP_DnaJ_Cys-rich_dom_sf"}]},{"database":"InterPro","id":"IPR036869","properties":[{"key":"EntryName","value":"J_dom_sf"}]},{"database":"NCBIfam","id":"NF008035","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010869","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010873","properties":[{"key":"EntryName","value":"dnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02349","properties":[{"key":"EntryName","value":"DnaJ_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43096:SF48","properties":[{"key":"EntryName","value":"CHAPERONE PROTEIN DNAJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43096","properties":[{"key":"EntryName","value":"DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00226","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01556","properties":[{"key":"EntryName","value":"DnaJ_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF27439","properties":[{"key":"EntryName","value":"DnaJ_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00684","properties":[{"key":"EntryName","value":"DnaJ_CXXCXGXG"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00625","properties":[{"key":"EntryName","value":"JDOMAIN"}]},{"database":"SMART","id":"SM00271","properties":[{"key":"EntryName","value":"DnaJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46565","properties":[{"key":"EntryName","value":"Chaperone J-domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57938","properties":[{"key":"EntryName","value":"DnaJ/Hsp40 cysteine-rich domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49493","properties":[{"key":"EntryName","value":"HSP40/DnaJ peptide-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00636","properties":[{"key":"EntryName","value":"DNAJ_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50076","properties":[{"key":"EntryName","value":"DNAJ_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51188","properties":[{"key":"EntryName","value":"ZF_CR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEKRDYYDVLGVGRDASDDEIKKAYRKLSKKYHPDINKAPDAEAKFKEVTEAYEALSDPQKRAAYDQYGHAGMNGGFGGGAGAGQGFGGFGGGAEGFGGFDDIFSSFFGGGARQQPNGPRQGSDLQYRMDLKFEEAVFGKETKISYSREAECHTCHGSGAKPGTSAETCHKCHGAGQIQVERQTPLGRMMSRETCDVCGGTGKEIKSKCDTCHGTGREEERHTVKVKVPAGVEDGQQMRLQGQGEAGSNGGPYGDLFIVFRVAPSDEFERDGAQIFVEVPISFVQAALGDEIEVNTVHGPVKLKIPAGTQTNTVFRLRGKGAPKLHGTGNGDQKVTVNVVTPKSLNSKQRDALKAFAVASGDSVNPQDNNLFDKILNKKHKK","length":383,"molWeight":41132,"crc64":"3D71B3C4419EAF59","md5":"3CD8B72D39458602D401011D2C72D58B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Repeat":4,"Zinc finger":1,"Binding site":8},"uniParcId":"UPI0000129580"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q93CX7","uniProtkbId":"UPP_LATSK","entryAudit":{"firstPublicDate":"2002-08-30","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-12-01","entryVersion":94,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Uracil phosphoribosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"2.4.2.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UMP pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UPRTase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"upp"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13017"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.9","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Allosterically activated by GTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Belongs to the UPRTase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Uracil phosphoribosyltransferase","featureId":"PRO_0000120839"},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}}],"keywords":[{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"11832506","citationType":"journal article","authors":["Dudez A.-M.","Chaillou S.","Hissler L.","Stentz R.","Champomier-Verges M.-C.","Alpert C.-A.","Zagorec M."],"citationCrossReferences":[{"database":"PubMed","id":"11832506"},{"database":"DOI","id":"10.1099/00221287-148-2-421"}],"title":"Physical and genetic map of the Lactobacillus sakei 23K chromosome.","publicationDate":"2002","journal":"Microbiology","firstPage":"421","lastPage":"431","volume":"148"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF401665","properties":[{"key":"ProteinId","value":"AAL00948.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_011374832.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP017931.1"}]},{"database":"AlphaFoldDB","id":"Q93CX7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q93CX7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"57133990","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00574","properties":[{"key":"RectionId","value":"UER00636"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004845","properties":[{"key":"GoTerm","value":"F:uracil phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044206","properties":[{"key":"GoTerm","value":"P:UMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006223","properties":[{"key":"GoTerm","value":"P:uracil salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000003","properties":[{"key":"EntryName","value":"Uracil phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01218_B","properties":[{"key":"EntryName","value":"Upp_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR034332","properties":[{"key":"EntryName","value":"Upp_B"}]},{"database":"InterPro","id":"IPR005765","properties":[{"key":"EntryName","value":"UPRT"}]},{"database":"InterPro","id":"IPR050054","properties":[{"key":"EntryName","value":"UPRTase/APRTase"}]},{"database":"NCBIfam","id":"NF001097","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01091","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315:SF4","properties":[{"key":"EntryName","value":"URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14681","properties":[{"key":"EntryName","value":"UPRTase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKFTVLNHPLIQHKLTIIRNKNTGTKVFREVANEIAELMVYEITRDLAMEDVEVETPMGPAIEKQLSGKKLAVVPILRAGLGMVDGVLELIPAAKVGHIGMYRDEKTLQPHEYFVKLPTDIDQRQLFIVDPMLATGGSAIMAIDALKKRGATSMRLVVLVAAPEGVKAVQEAHPDVDIYAAGLDDGLNEEGYIYPGLGDAGDRLFGTK","length":209,"molWeight":22776,"crc64":"0F67971E1825F6F9","md5":"6A499A1C700A392C03950CA4D2D55C53"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":6},"uniParcId":"UPI0000137D27"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O85235","uniProtkbId":"PTH_LATSK","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1998-11-01","entryVersion":94,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Peptidyl-tRNA hydrolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Pth"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"3.1.1.29"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"pth"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino acid + a tRNA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54448"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:13883"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59874"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:138191"}],"ecNumber":"3.1.1.29","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Belongs to the PTH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Peptidyl-tRNA hydrolase","featureId":"PRO_0000187756"},{"type":"Active site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}]},{"type":"Site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00083"}]}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CBO5E3GROFRTB","citationType":"submission","authors":["Malleret C.","Lauret R.","Ehrlich S.D.","Morel-Deville F.","Zagorec M."],"title":"Construction and analysis of a stable Lactobacillus sake mutant deficient in L-lactate dehydrogenase.","publicationDate":"MAR-1998","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"207","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF054624","properties":[{"key":"ProteinId","value":"AAD03811.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O85235","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O85235","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004045","properties":[{"key":"GoTerm","value":"F:peptidyl-tRNA hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0072344","properties":[{"key":"GoTerm","value":"P:rescue of stalled cytosolic ribosome"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00462","properties":[{"key":"EntryName","value":"PTH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1470:FF:000001","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1470","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00083","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001328","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro"}]},{"database":"InterPro","id":"IPR018171","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_CS"}]},{"database":"InterPro","id":"IPR036416","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_sf"}]},{"database":"NCBIfam","id":"TIGR00447","properties":[{"key":"EntryName","value":"pth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR17224","properties":[{"key":"EntryName","value":"PEPTIDYL-TRNA HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR17224:SF1","properties":[{"key":"EntryName","value":"PEPTIDYL-TRNA HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01195","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53178","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01195","properties":[{"key":"EntryName","value":"PEPT_TRNA_HYDROL_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01196","properties":[{"key":"EntryName","value":"PEPT_TRNA_HYDROL_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKMIVGLGNPGSKYAKTKHNIGFMVIDQLCEKYNVTLNKHDFEAEYGSFKYEGETVLLVKPLTFMNDSGRSVGPLMSYYQVGIDELLVIQDDMDLTMGKLRLRQKGSAGGHNGIKSIIAHTKSQTFKRLKIGIQHPQKSTVVNWVLTPFDKDGAPVINQAIDQACEESTTGVKMTTL","length":177,"molWeight":19641,"crc64":"FB4A4C1751AC6CFC","md5":"8B93A6DBD40F0EF0002126171E68B7D3"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":4,"Site":2},"uniParcId":"UPI000013291F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P50934","uniProtkbId":"LDH_LATSK","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"1996-10-01","entryVersion":123,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"L-lactate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"L-LDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"1.1.1.27"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"ldh"},"synonyms":[{"value":"ldhL"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Catalyzes the conversion of lactate to pyruvate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-lactate + NAD(+) = pyruvate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23444"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16651"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.27","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Allosterically activated by fructose 1,6-bisphosphate (FBP)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the LDH/MDH superfamily. LDH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"L-lactate dehydrogenase","featureId":"PRO_0000168360"},{"type":"Active site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}]},{"type":"Binding site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00488"}]}],"keywords":[{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9P8DPN052V1OA","citationType":"submission","authors":["van den Berg D.J.C.","Verbiest A.","Costello M.","Ledeboer A.M.","Verrips C."],"title":"Cloning and sequencing of the L-ldh gene from Lactobacillus sake 0-1.","publicationDate":"JUN-1995","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"CBS 532.92 / 0-1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9884224","citationType":"journal article","authors":["Malleret C.","Lauret R.","Ehrlich S.D.","Morel-Deville F.","Zagorec M."],"citationCrossReferences":[{"database":"PubMed","id":"9884224"},{"database":"DOI","id":"10.1099/00221287-144-12-3327"}],"title":"Disruption of the sole ldhL gene in Lactobacillus sakei prevents the production of both L- and D-lactate.","publicationDate":"1998","journal":"Microbiology","firstPage":"3327","lastPage":"3333","volume":"144"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"207","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U26688","properties":[{"key":"ProteinId","value":"AAA67994.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF054624","properties":[{"key":"ProteinId","value":"AAD03812.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"P50934","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P50934","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00554","properties":[{"key":"RectionId","value":"UER00611"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004459","properties":[{"key":"GoTerm","value":"F:L-lactate dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006089","properties":[{"key":"GoTerm","value":"P:lactate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd05291","properties":[{"key":"EntryName","value":"HicDH_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000018","properties":[{"key":"EntryName","value":"Malate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.110.10","properties":[{"key":"EntryName","value":"Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00488","properties":[{"key":"EntryName","value":"Lactate_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001557","properties":[{"key":"EntryName","value":"L-lactate/malate_DH"}]},{"database":"InterPro","id":"IPR011304","properties":[{"key":"EntryName","value":"L-lactate_DH"}]},{"database":"InterPro","id":"IPR018177","properties":[{"key":"EntryName","value":"L-lactate_DH_AS"}]},{"database":"InterPro","id":"IPR022383","properties":[{"key":"EntryName","value":"Lactate/malate_DH_C"}]},{"database":"InterPro","id":"IPR001236","properties":[{"key":"EntryName","value":"Lactate/malate_DH_N"}]},{"database":"InterPro","id":"IPR015955","properties":[{"key":"EntryName","value":"Lactate_DH/Glyco_Ohase_4_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01771","properties":[{"key":"EntryName","value":"L-LDH-NAD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF000824","properties":[{"key":"EntryName","value":"PRK00066.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004863","properties":[{"key":"EntryName","value":"PRK06223.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128","properties":[{"key":"EntryName","value":"L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128:SF16","properties":[{"key":"EntryName","value":"L-LACTATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02866","properties":[{"key":"EntryName","value":"Ldh_1_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00056","properties":[{"key":"EntryName","value":"Ldh_1_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000102","properties":[{"key":"EntryName","value":"Lac_mal_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00086","properties":[{"key":"EntryName","value":"LLDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF56327","properties":[{"key":"EntryName","value":"LDH C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00064","properties":[{"key":"EntryName","value":"L_LDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANIEKDHQKVILVGDGAVGSYYAYALTLQGIAQEVGIVDIFKEKTQGDAIDLSDALAFTSPKKIYAAEYSDAKDADVVVITAGAPQKPGETRLDLVSKNLKILKTIVDPIVESGFNGIFLVAANPVDILTYATWKLSGFPKERVIGSGTSLDSARFRKDIAEMVNVDARSVHAYIMGEHGDTEFPVWSHANIGGIKISEWVKAHPEVKEEELVKIFESVRDAAYTIINLKGATFYGIGTALARITKAILDDENAVLPLSVFMDGQYGLNDIFIGSPAVINRSGITNILEIPLTDHEMESMHKSAKQLKDIVTKAFEELDIETRQ","length":325,"molWeight":35501,"crc64":"B6117BBD5AC4B0BF","md5":"3D4F4D8291222A3AA56902184F09B78A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":15,"Modified residue":1},"uniParcId":"UPI000012E339"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O07126","uniProtkbId":"PT1_LATSK","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1997-07-01","entryVersion":120,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"Phosphoenolpyruvate-protein phosphotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"2.7.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"Phosphotransferase system, enzyme I"}}]},"genes":[{"geneName":{"value":"ptsI"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23880"},{"database":"Rhea","id":"RHEA-COMP:9745"},{"database":"Rhea","id":"RHEA-COMP:9746"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:29979"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:64837"}],"ecNumber":"2.7.3.9","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"value":"The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PEP-utilizing enzyme family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate-protein phosphotransferase","featureId":"PRO_0000147072"},{"type":"Active site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Tele-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}]},{"type":"Active site","location":{"start":{"value":503,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}]},{"type":"Binding site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P23533"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P08839"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P23533"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0598","category":"Biological process","name":"Phosphotransferase system"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9172326","citationType":"journal article","authors":["Stentz R.","Lauret R.","Ehrlich S.D.","Morel-Deville F.","Zagorec M."],"citationCrossReferences":[{"database":"PubMed","id":"9172326"},{"database":"DOI","id":"10.1128/aem.63.6.2111-2116.1997"}],"title":"Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"2111","lastPage":"2116","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"160*1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U82366","properties":[{"key":"ProteinId","value":"AAC45391.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_011375154.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CABFKU010000004.1"}]},{"database":"AlphaFoldDB","id":"O07126","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O07126","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AADPLMI","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008965","properties":[{"key":"GoTerm","value":"F:phosphoenolpyruvate-protein phosphotransferase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0009401","properties":[{"key":"GoTerm","value":"P:phosphoenolpyruvate-dependent sugar phosphotransferase system"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.20.20.60:FF:000007","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate-protein phosphotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.60","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate-binding domains"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.10","properties":[{"key":"EntryName","value":"Phosphohistidine domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.274.10","properties":[{"key":"EntryName","value":"PtsI, HPr-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008279","properties":[{"key":"EntryName","value":"PEP-util_enz_mobile_dom"}]},{"database":"InterPro","id":"IPR050499","properties":[{"key":"EntryName","value":"PEP-utilizing_PTS_enzyme"}]},{"database":"InterPro","id":"IPR018274","properties":[{"key":"EntryName","value":"PEP_util_AS"}]},{"database":"InterPro","id":"IPR000121","properties":[{"key":"EntryName","value":"PEP_util_C"}]},{"database":"InterPro","id":"IPR023151","properties":[{"key":"EntryName","value":"PEP_util_CS"}]},{"database":"InterPro","id":"IPR036637","properties":[{"key":"EntryName","value":"Phosphohistidine_dom_sf"}]},{"database":"InterPro","id":"IPR024692","properties":[{"key":"EntryName","value":"PTS_EI"}]},{"database":"InterPro","id":"IPR006318","properties":[{"key":"EntryName","value":"PTS_EI-like"}]},{"database":"InterPro","id":"IPR008731","properties":[{"key":"EntryName","value":"PTS_EIN"}]},{"database":"InterPro","id":"IPR036618","properties":[{"key":"EntryName","value":"PtsI_HPr-bd_sf"}]},{"database":"InterPro","id":"IPR015813","properties":[{"key":"EntryName","value":"Pyrv/PenolPyrv_kinase-like_dom"}]},{"database":"InterPro","id":"IPR040442","properties":[{"key":"EntryName","value":"Pyrv_kinase-like_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01417","properties":[{"key":"EntryName","value":"PTS_I_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46244","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46244:SF3","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05524","properties":[{"key":"EntryName","value":"PEP-utilisers_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00391","properties":[{"key":"EntryName","value":"PEP-utilizers"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02896","properties":[{"key":"EntryName","value":"PEP-utilizers_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000732","properties":[{"key":"EntryName","value":"PTS_enzyme_I"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01736","properties":[{"key":"EntryName","value":"PHPHTRNFRASE"}]},{"database":"SUPFAM","id":"SSF47831","properties":[{"key":"EntryName","value":"Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51621","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate/pyruvate domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52009","properties":[{"key":"EntryName","value":"Phosphohistidine domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00742","properties":[{"key":"EntryName","value":"PEP_ENZYMES_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00370","properties":[{"key":"EntryName","value":"PEP_ENZYMES_PHOS_SITE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKLRGIAASDGIATAKAYMLVQPDLSFSKSTISDSEKEINRLHKALQDSTSDLETIRKIAAESLGEEEAQVFDAHMMILADPEFTGAIEGKINDDKVNAEQALKEVADLFVATFESMTNNAYMQERAADIKDVTKRVLSHLLGVTLPNPALIDEEVIVIAHDLTPSDTAQLNGKFVKAFVTDVGGRTSHSAIMARSLEIPAIVGTETVTQDVKAGDLLIVDGINGDVVLDPTDADIAEYDVKAQAFADQKAEWEKLKNEKSVTKDGKTFTVAANIGTPKDLAGVLENGSEAIGLYRTEFLYMDSAELPSEDDQFEAYKSVLEGMDGKPVVVRTMDIGGDKKLPYLPLPEEMNPFLGYRAIRISLDRDDIFRTQLRALLRASNYGKLRIMFPMIATVAEFRQAKGILEDEKAKLIAAGQTVSDDLQVGMMVEIPASAVLANQFAKEVDFFSIGTNDLIQYTMAADRMNERVSYLYQPYNPAILRLIKNVIDASHKEGKWTGMCGEAAGDSIMAPLLVGMGLDEFSMSATSVLRVRSLMKRLDTTELTDLVETAVNVNTSNEENQKLVEDFMKDR","length":574,"molWeight":63009,"crc64":"5544473E7292DBF1","md5":"0D84F1D04DE08D4622A84EEE36E636C0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":6},"uniParcId":"UPI0000132875"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P30265","uniProtkbId":"CATA_LATSK","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1999-07-15","entryVersion":105,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Catalase"},"ecNumbers":[{"value":"1.11.1.6"}]}},"genes":[{"geneName":{"value":"katA"}}],"comments":[{"texts":[{"value":"Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.6","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10013"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the catalase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"Catalase","featureId":"PRO_0000084989"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10013"}]},{"type":"Active site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10013"}]},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0575","category":"Molecular function","name":"Peroxidase"}],"references":[{"referenceNumber":1,"citation":{"id":"1575485","citationType":"journal article","authors":["Knauf H.J.","Vogel R.F.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"1575485"},{"database":"DOI","id":"10.1128/aem.58.3.832-839.1992"}],"title":"Cloning, sequence, and phenotypic expression of katA, which encodes the catalase of Lactobacillus sake LTH677.","publicationDate":"1992","journal":"Appl. Environ. Microbiol.","firstPage":"832","lastPage":"839","volume":"58"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH677","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9546173","citationType":"journal article","authors":["Hertel C.","Schmidt G.","Fischer M.","Oellers K.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"9546173"},{"database":"DOI","id":"10.1128/aem.64.4.1359-1365.1998"}],"title":"Oxygen-dependent regulation of the expression of the catalase gene katA of Lactobacillus sakei LTH677.","publicationDate":"1998","journal":"Appl. Environ. Microbiol.","firstPage":"1359","lastPage":"1365","volume":"64"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","SEQUENCE REVISION"],"referenceComments":[{"value":"LTH677","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M84015","properties":[{"key":"ProteinId","value":"AAC19139.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T09652","properties":[{"key":"EntryName","value":"T09652"}]},{"database":"AlphaFoldDB","id":"P30265","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P30265","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AAARWDH","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042542","properties":[{"key":"GoTerm","value":"P:response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd08156","properties":[{"key":"EntryName","value":"catalase_clade_3"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.180.10:FF:000001","properties":[{"key":"EntryName","value":"Catalase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.180.10","properties":[{"key":"EntryName","value":"Catalase core domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018028","properties":[{"key":"EntryName","value":"Catalase"}]},{"database":"InterPro","id":"IPR040333","properties":[{"key":"EntryName","value":"Catalase_3"}]},{"database":"InterPro","id":"IPR024708","properties":[{"key":"EntryName","value":"Catalase_AS"}]},{"database":"InterPro","id":"IPR024711","properties":[{"key":"EntryName","value":"Catalase_clade1/3"}]},{"database":"InterPro","id":"IPR011614","properties":[{"key":"EntryName","value":"Catalase_core"}]},{"database":"InterPro","id":"IPR002226","properties":[{"key":"EntryName","value":"Catalase_haem_BS"}]},{"database":"InterPro","id":"IPR010582","properties":[{"key":"EntryName","value":"Catalase_immune_responsive"}]},{"database":"InterPro","id":"IPR020835","properties":[{"key":"EntryName","value":"Catalase_sf"}]},{"database":"PANTHER","id":"PTHR11465","properties":[{"key":"EntryName","value":"CATALASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11465:SF9","properties":[{"key":"EntryName","value":"CATALASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00199","properties":[{"key":"EntryName","value":"Catalase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06628","properties":[{"key":"EntryName","value":"Catalase-rel"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF038928","properties":[{"key":"EntryName","value":"Catalase_clade1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00067","properties":[{"key":"EntryName","value":"CATALASE"}]},{"database":"SMART","id":"SM01060","properties":[{"key":"EntryName","value":"Catalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56634","properties":[{"key":"EntryName","value":"Heme-dependent catalase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00437","properties":[{"key":"EntryName","value":"CATALASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00438","properties":[{"key":"EntryName","value":"CATALASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51402","properties":[{"key":"EntryName","value":"CATALASE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNQLTTNEGQPWADNQHSQTAGQRGPVLIQDYQLLEKLAHFNRERIPERVVHAKGAGAKGYFKVTKDMSAYTKAAVFSGVGKKTPLITRFSQVAGEAGYPDTYRDVRGFAVKFYTEEGNYDIVGNNTPVFFVNDPLKFPDFIHSQKRDPRTHARSQDMQWDFWSLSPESVHQVTILMSDRGIPASYRMMHGFGSHTFKWVNAQGEQFWVKYHFKTNQGIHNLSNELADELAGKDTDYLQNDLFDAIETGDYPSWTVAVQLVPYEDGLNYPQDIFDVTKVISQKDYPLIEIGQMVLDENPTNNFEDIQELAFSPANLVPGIEASPDKLLQGRLFGYKDAERYRLGANYEQLPVNRPKVPVHNYERDGAMAQNQATGVNYEPNSQDGPTEVPAAKIHGDQLSGTTGNFSADPDYYSAAGKLYRLLSADEQTRLIENIRMNLGQVTKPEIQIREVKQFYQADPEYGRRVATSVKLRFSSV","length":478,"molWeight":54076,"crc64":"85952A05DB16EF3D","md5":"A07D59569BF26C0514B66F69A2AF420E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":1,"Active site":2,"Binding site":1},"uniParcId":"UPI0000127065"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P35618","secondaryAccessions":["Q57121"],"uniProtkbId":"SAKP_LATSK","entryAudit":{"firstPublicDate":"1994-06-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-08-29","entryVersion":100,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Bacteriocin sakacin-P"}},"alternativeNames":[{"fullName":{"value":"Sakacin 674"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"sakP"},"synonyms":[{"value":"sakR"},{"value":"sppA"}]}],"comments":[{"texts":[{"value":"Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacteriocin class IIA/YGNGV family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Propeptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8138128"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"featureId":"PRO_0000002751"},{"type":"Chain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Bacteriocin sakacin-P","featureId":"PRO_0000002752"},{"type":"Disulfide bond","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14516192"}]},{"type":"Beta strand","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1OG7"}]},{"type":"Beta strand","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1OG7"}]},{"type":"Turn","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1OG7"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1OG7"}]},{"type":"Turn","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1OG7"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0044","category":"Molecular function","name":"Antibiotic"},{"id":"KW-0929","category":"Molecular function","name":"Antimicrobial"},{"id":"KW-0078","category":"Molecular function","name":"Bacteriocin"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"8180701","citationType":"journal article","authors":["Tichaczek P.S.","Vogel R.F.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"8180701"},{"database":"DOI","id":"10.1099/13500872-140-2-361"}],"title":"Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673.","publicationDate":"1994","journal":"Microbiology","firstPage":"361","lastPage":"367","volume":"140"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH673","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8138128","citationType":"journal article","authors":["Holck A.L.","Axelsson L.","Huehne K.","Kroeckel L."],"citationCrossReferences":[{"database":"PubMed","id":"8138128"},{"database":"DOI","id":"10.1111/j.1574-6968.1994.tb06629.x"}],"title":"Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sake Lb674.","publicationDate":"1994","journal":"FEMS Microbiol. Lett.","firstPage":"143","lastPage":"150","volume":"115"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 19-61","CHARACTERIZATION"],"referenceComments":[{"value":"Lb674","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"8704983","citationType":"journal article","authors":["Huehne K.","Axelsson L.","Holck A.","Kroeckel L."],"citationCrossReferences":[{"database":"PubMed","id":"8704983"},{"database":"DOI","id":"10.1099/13500872-142-6-1437"}],"title":"Analysis of the sakacin P gene cluster from Lactobacillus sake Lb674 and its expression in sakacin-negative Lb. sake strains.","publicationDate":"1996","journal":"Microbiology","firstPage":"1437","lastPage":"1448","volume":"142"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"Lb674","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"CI-F800P1I4RS9QN","citationType":"journal article","authors":["Tichaczek P.S.","Nissen-Meyer J.","Nes I.F.","Vogel R.F.","Hammes W.P."],"title":"Characterization of the bacteriocins curvacin A from Lactobacillus curvatus LTH1174 and sakacin P from L. sake LTH673.","publicationDate":"1992","journal":"Syst. Appl. Microbiol.","firstPage":"460","lastPage":"465","volume":"15"},"referencePositions":["PROTEIN SEQUENCE OF 19-59","CHARACTERIZATION"],"referenceComments":[{"value":"LTH673","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"14516192","citationType":"journal article","authors":["Uteng M.","Hauge H.H.","Markwick P.R.","Fimland G.","Mantzilas D.","Nissen-Meyer J.","Muhle-Goll C."],"citationCrossReferences":[{"database":"PubMed","id":"14516192"},{"database":"DOI","id":"10.1021/bi034572i"}],"title":"Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge.","publicationDate":"2003","journal":"Biochemistry","firstPage":"11417","lastPage":"11426","volume":"42"},"referencePositions":["STRUCTURE BY NMR OF 19-61","DISULFIDE BOND"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X75081","properties":[{"key":"ProteinId","value":"CAA52974.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"Z25816","properties":[{"key":"ProteinId","value":"CAA81064.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"Z48542","properties":[{"key":"ProteinId","value":"CAA88428.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF002276","properties":[{"key":"ProteinId","value":"AAB93970.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S57911","properties":[{"key":"EntryName","value":"S38508"}]},{"database":"RefSeq","id":"WP_004271264.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP017566.1"}]},{"database":"PDB","id":"1OG7","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=19-61"}]},{"database":"PDB","id":"1OHM","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=19-61"}]},{"database":"PDB","id":"1OHN","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=19-61"}]},{"database":"AlphaFoldDB","id":"P35618","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P35618","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P35618","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"1.C.24.1.2","properties":[{"key":"FamilyName","value":"the pediocin (pediocin) family"}]},{"database":"EvolutionaryTrace","id":"P35618","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0042742","properties":[{"key":"GoTerm","value":"P:defense response to bacterium"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.5.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002633","properties":[{"key":"EntryName","value":"Bacteriocin_IIa"}]},{"database":"InterPro","id":"IPR023384","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_CS"}]},{"database":"InterPro","id":"IPR023388","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_dom_sf"}]},{"database":"Pfam","id":"PF01721","properties":[{"key":"EntryName","value":"Bacteriocin_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS60030","properties":[{"key":"EntryName","value":"BACTERIOCIN_IIA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKFIELSLKEVTAITGGKYYGNGVHCGKHSCTVDWGTAIGNIGNNAAANWATGGNAGWNK","length":61,"molWeight":6385,"crc64":"B7BF14DCDD28A73D","md5":"6DF434D083BFD8C837217253CEFB8596"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Propeptide":1,"Chain":1,"Disulfide bond":1,"Beta strand":2,"Turn":2,"Helix":1},"uniParcId":"UPI00000013AD"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O07125","uniProtkbId":"PTHP_LATSK","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1997-07-01","entryVersion":123,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Phosphocarrier protein HPr"}},"alternativeNames":[{"fullName":{"value":"Histidine-containing protein"}}]},"genes":[{"geneName":{"value":"ptsH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Phosphorylation on Ser-46 inhibits the phosphoryl transfer from enzyme I to HPr"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the HPr family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Phosphocarrier protein HPr","featureId":"PRO_0000107859"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"HPr","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00681"}]},{"type":"Active site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Pros-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00681"}]},{"type":"Modified residue","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Phosphoserine; by HPrK/P","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00681"}]}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0598","category":"Biological process","name":"Phosphotransferase system"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9172326","citationType":"journal article","authors":["Stentz R.","Lauret R.","Ehrlich S.D.","Morel-Deville F.","Zagorec M."],"citationCrossReferences":[{"database":"PubMed","id":"9172326"},{"database":"DOI","id":"10.1128/aem.63.6.2111-2116.1997"}],"title":"Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"2111","lastPage":"2116","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"160*1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U82366","properties":[{"key":"ProteinId","value":"AAC45390.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_004265632.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP017931.1"}]},{"database":"AlphaFoldDB","id":"O07125","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O07125","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"49610884","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AAEFPCQ","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"CDD","id":"cd00367","properties":[{"key":"EntryName","value":"PTS-HPr_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1340.10","properties":[{"key":"EntryName","value":"HPr-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050399","properties":[{"key":"EntryName","value":"HPr"}]},{"database":"InterPro","id":"IPR000032","properties":[{"key":"EntryName","value":"HPr-like"}]},{"database":"InterPro","id":"IPR035895","properties":[{"key":"EntryName","value":"HPr-like_sf"}]},{"database":"InterPro","id":"IPR001020","properties":[{"key":"EntryName","value":"PTS_HPr_His_P_site"}]},{"database":"InterPro","id":"IPR002114","properties":[{"key":"EntryName","value":"PTS_HPr_Ser_P_site"}]},{"database":"NCBIfam","id":"NF010352","properties":[{"key":"EntryName","value":"PRK13780.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01003","properties":[{"key":"EntryName","value":"PTS_HPr_family"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33705","properties":[{"key":"EntryName","value":"PHOSPHOCARRIER PROTEIN HPR"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33705:SF2","properties":[{"key":"EntryName","value":"PHOSPHOCARRIER PROTEIN NPR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00381","properties":[{"key":"EntryName","value":"PTS-HPr"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00107","properties":[{"key":"EntryName","value":"PHOSPHOCPHPR"}]},{"database":"SUPFAM","id":"SSF55594","properties":[{"key":"EntryName","value":"HPr-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51350","properties":[{"key":"EntryName","value":"PTS_HPR_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00369","properties":[{"key":"EntryName","value":"PTS_HPR_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00589","properties":[{"key":"EntryName","value":"PTS_HPR_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKRDFHVVADTGIHARPATLLVQTASKFNSDVNLEYKGKSVNLKSIMGVMSLGVGQGADVTISAEGADEADAINAIEETMKKEGLSE","length":88,"molWeight":9338,"crc64":"4843D6E17C4ABB6F","md5":"3AA8F79536F10659FB64152449B8C4FC"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"ACTIVITY REGULATION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":1,"Modified residue":1},"uniParcId":"UPI00001328F3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O53089","uniProtkbId":"OTCC_LATSK","entryAudit":{"firstPublicDate":"2003-07-11","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":104,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Ornithine carbamoyltransferase, catabolic"},"shortNames":[{"value":"OTCase"}],"ecNumbers":[{"value":"2.1.3.3"}]}},"genes":[{"geneName":{"value":"arcB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-ornithine = L-citrulline + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19513"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57743"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.3"}},{"texts":[{"value":"Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Ornithine carbamoyltransferase, catabolic","featureId":"PRO_0000112938"},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}}],"keywords":[{"id":"KW-0056","category":"Biological process","name":"Arginine metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9696763","citationType":"journal article","authors":["Zuniga M.","Champomier-Verges M.-C.","Zagorec M.","Perez-Martinez G."],"citationCrossReferences":[{"database":"PubMed","id":"9696763"},{"database":"DOI","id":"10.1128/jb.180.16.4154-4159.1998"}],"title":"Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sakei.","publicationDate":"1998","journal":"J. Bacteriol.","firstPage":"4154","lastPage":"4159","volume":"180"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ001330","properties":[{"key":"ProteinId","value":"CAA04683.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46742","properties":[{"key":"EntryName","value":"T46742"}]},{"database":"AlphaFoldDB","id":"O53089","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O53089","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AACFDFK","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"UniPathway","id":"UPA00254","properties":[{"key":"RectionId","value":"UER00365"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004585","properties":[{"key":"GoTerm","value":"F:ornithine carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000008","properties":[{"key":"EntryName","value":"Ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01109","properties":[{"key":"EntryName","value":"OTCase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR002292","properties":[{"key":"EntryName","value":"Orn/put_carbamltrans"}]},{"database":"InterPro","id":"IPR024904","properties":[{"key":"EntryName","value":"OTCase_ArgI"}]},{"database":"NCBIfam","id":"TIGR00658","properties":[{"key":"EntryName","value":"orni_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF1","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00102","properties":[{"key":"EntryName","value":"OTCASE"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNSVFQGRSLLAEKDFTKSELEYLIDFSLHLKDLKKKGIPHHYLEGKNIALLFEKNSTRTRAAFTTAAIDLGAHPEFLGKNDIQLGKKESVEDTAKVLGSMFDGIEFRALAKVVEDLAKYSGVPVWNGLTDEWHPTQMIADFMTVKENFGKLKGVTLTYVGDGRNNMANSLLVTGSMLGVNIHIVAPDSLQPTQEVRDLAEGYAKETGSKNMITSDVDAGVKGSDVLYTDVWVSMGEEDKFEERVNLLKPYQINMDMVKKTGNENMIIMHCLPAFHDIETEYGKKIDEQFGIQEMEITDEAFRSKYARQFEEAENRMHSIKAIMAATLGNLFIPQA","length":337,"molWeight":37774,"crc64":"1C252EB5D0342D53","md5":"4A37C26C78AA60016927AAF527E29243"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":9},"uniParcId":"UPI00000AF359"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48846","uniProtkbId":"BGAL_LATSK","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":96,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Beta-galactosidase large subunit"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Beta-gal large subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q02603"}],"value":"3.2.1.23"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8574399"}],"value":"lacL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8574399"}],"value":"Component of a beta-galactosidase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.","ecNumber":"3.2.1.23","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q02603"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Heterodimer of a large (LacL) and a small subunit (LacM)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"Beta-galactosidase large subunit","featureId":"PRO_0000057670"},{"type":"Active site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":533,"modifier":"EXACT"},"end":{"value":533,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"8574399","citationType":"journal article","authors":["Obst M.","Meding E.R.","Vogel R.F.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"8574399"},{"database":"DOI","id":"10.1099/13500872-141-12-3059"}],"title":"Two genes encoding the beta-galactosidase of Lactobacillus sake.","publicationDate":"1995","journal":"Microbiology","firstPage":"3059","lastPage":"3066","volume":"141"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","SUBUNIT"],"referenceComments":[{"value":"ATCC 15521 / DSM 20017 / JCM 1157 / CCUG 30501 / CIP 103139 / KCTC 3603 / NBRC 15893 / NCIMB 13090 / T.S","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X82287","properties":[{"key":"ProteinId","value":"CAA57730.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_025015980.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CEMAWX010000007.1"}]},{"database":"AlphaFoldDB","id":"Q48846","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48846","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH2","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 2"}]},{"database":"GeneID","id":"57132632","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"ACVWDYF","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0009341","properties":[{"key":"GoTerm","value":"C:beta-galactosidase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004565","properties":[{"key":"GoTerm","value":"F:beta-galactosidase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0005990","properties":[{"key":"GoTerm","value":"P:lactose catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"2.60.120.260","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050347","properties":[{"key":"EntryName","value":"Bact_Beta-galactosidase"}]},{"database":"InterPro","id":"IPR036156","properties":[{"key":"EntryName","value":"Beta-gal/glucu_dom_sf"}]},{"database":"InterPro","id":"IPR008979","properties":[{"key":"EntryName","value":"Galactose-bd-like_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR006101","properties":[{"key":"EntryName","value":"Glyco_hydro_2"}]},{"database":"InterPro","id":"IPR023232","properties":[{"key":"EntryName","value":"Glyco_hydro_2_AS"}]},{"database":"InterPro","id":"IPR006103","properties":[{"key":"EntryName","value":"Glyco_hydro_2_cat"}]},{"database":"InterPro","id":"IPR023230","properties":[{"key":"EntryName","value":"Glyco_hydro_2_CS"}]},{"database":"InterPro","id":"IPR006104","properties":[{"key":"EntryName","value":"Glyco_hydro_2_N"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR006102","properties":[{"key":"EntryName","value":"Ig-like_GH2"}]},{"database":"PANTHER","id":"PTHR46323","properties":[{"key":"EntryName","value":"BETA-GALACTOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46323:SF2","properties":[{"key":"EntryName","value":"BETA-GALACTOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00703","properties":[{"key":"EntryName","value":"Glyco_hydro_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02836","properties":[{"key":"EntryName","value":"Glyco_hydro_2_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02837","properties":[{"key":"EntryName","value":"Glyco_hydro_2_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00132","properties":[{"key":"EntryName","value":"GLHYDRLASE2"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49303","properties":[{"key":"EntryName","value":"beta-Galactosidase/glucuronidase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49785","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00719","properties":[{"key":"EntryName","value":"GLYCOSYL_HYDROL_F2_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00608","properties":[{"key":"EntryName","value":"GLYCOSYL_HYDROL_F2_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQPNIQWLDTPAVFRVGQLPAHSDHRYYATLAEMAQQQSSFEQSLNGTWQFHYSVNAASRPKSFYELAFDAQDFEPITVPQHIELAGYEQLHYINTMYPWEGHYYRRPAFSTSDDKQHLGMFSEADYNPVGSYLHHFDLTPALRNQRVIIRFEGVEQAMYVWLNGQFIGYAEDSFTPSEFDLTPYLKETDNCLAVEVHKRSSAAFIEDQDFFRFFGIFRDVKLLAKPRTHLEDLWVIPEYDVVQQTGQVKLRLQFSGDENRVHLRIRDQHQIILTADLTSGAQVNDLYKMPELVQAWSNQTPNLYTLELEVVDQAGETIEISQQPFGFRKIEIKDKVMLLNGKRLVINGVNRHEWHPETGRTITAEDEAWDIACMQRNHINAVRTSHYPDRLSFYNGCDQAGIYMMAETNLESHGSWQKMGAVEPSWNVPGSYDEWEAATLDRARTNFETFKNHVSILFWSLGNESYAGSVLEKMNAYYKQQDPTRLVHYEGVFRAPEYKATISDVESRMYATPAEIKAYLDNAPQKPFILCEYMHDMGNSLGGMQSYIDLLSQYDMYQGGFIWDFIDQALLVTDPVTGQRELRYGGDFDDRPSDYEFSGDGLVFATRDEKPAMQEVRYYYGEHK","length":625,"molWeight":72457,"crc64":"C658A3C46136B886","md5":"89F55CDF676397D8EA64EDD682473C7D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2},"uniParcId":"UPI00001268E5"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O53092","uniProtkbId":"ARCD_LATSK","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":98,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2RNI5"}],"value":"Arginine/ornithine antiporter"}}},"genes":[{"geneName":{"value":"arcD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2RNI5"}],"value":"Catalyzes electroneutral exchange between L-arginine and L-ornithine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-ornithine(in) + L-arginine(out) = L-ornithine(out) + L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:34991"},{"database":"ChEBI","id":"CHEBI:32682"},{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2RNI5"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"Arginine/ornithine antiporter","featureId":"PRO_0000054238"},{"type":"Transmembrane","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":397,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-0029","category":"Biological process","name":"Amino-acid transport"},{"id":"KW-0050","category":"Biological process","name":"Antiport"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9696763","citationType":"journal article","authors":["Zuniga M.","Champomier-Verges M.-C.","Zagorec M.","Perez-Martinez G."],"citationCrossReferences":[{"database":"PubMed","id":"9696763"},{"database":"DOI","id":"10.1128/jb.180.16.4154-4159.1998"}],"title":"Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sakei.","publicationDate":"1998","journal":"J. Bacteriol.","firstPage":"4154","lastPage":"4159","volume":"180"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ001330","properties":[{"key":"ProteinId","value":"CAA04686.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46745","properties":[{"key":"EntryName","value":"T46745"}]},{"database":"AlphaFoldDB","id":"O53092","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O53092","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AADHNIM","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043858","properties":[{"key":"GoTerm","value":"F:arginine:ornithine antiporter activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0006527","properties":[{"key":"GoTerm","value":"P:L-arginine catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:1903826","properties":[{"key":"GoTerm","value":"P:L-arginine transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1740.10","properties":[{"key":"EntryName","value":"Amino acid/polyamine transporter I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002293","properties":[{"key":"EntryName","value":"AA/rel_permease1"}]},{"database":"InterPro","id":"IPR004754","properties":[{"key":"EntryName","value":"Amino_acid_antiprt"}]},{"database":"InterPro","id":"IPR050367","properties":[{"key":"EntryName","value":"APC_superfamily"}]},{"database":"InterPro","id":"IPR022461","properties":[{"key":"EntryName","value":"Arg/Orn_antiprt_ArcD"}]},{"database":"NCBIfam","id":"TIGR00905","properties":[{"key":"EntryName","value":"2A0302"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR03810","properties":[{"key":"EntryName","value":"arg_ornith_anti"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42770","properties":[{"key":"EntryName","value":"AMINO ACID TRANSPORTER-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42770:SF4","properties":[{"key":"EntryName","value":"ARGININE_ORNITHINE ANTIPORTER-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13520","properties":[{"key":"EntryName","value":"AA_permease_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006060","properties":[{"key":"EntryName","value":"AA_transporter"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTEEKPAKKIGLLALIALVISSSIGSGVFGLTSDLASASAPGPVLIAWVIVGFGILMLALSLNNLLMKEPELEGIFSYAEKGFGPFAGFISGWGYWLSAWLGNVTFATILMSALGYFFPIFKSRQNLPSILVASVLSWSLTYFVNRGVEGAAAINTLVTICKLIPLFVFIIFGIVLFKGHLFTQAFWNNMSSSFVAGDVMSQIKNCMMVMMWVFVGIEGASMLSARAEKKSDAGKATILGLVSLLAIYILASVLPYGYLTQDQLASIKQPAMLYIFEQMVGTWGGYFIGVGLIISILGAWLSWTMLPAETMLLMAKQNLLPAYFGRVNKKKAPTFALVVTAGLIQVFLFTLLFTTKAYNFAYSLCTASIIVCYMLVAAYQIKYSWAHLQEKGNRQQLLIGVLALLFEIAGILMAGVSYLLLCFIAYIPGIYFYGRARKNNGHQHFLSKGEWLITTIIVIGAIIGIWLVVSGKIVI","length":475,"molWeight":51881,"crc64":"8E91A01F6A2203CC","md5":"207219CC4C737E12EC5EEA15539C78DF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":12},"uniParcId":"UPI0000125DAC"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P80953","uniProtkbId":"BAVA_LATSK","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-11-01","entryVersion":60,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Bacteriocin bavaricin-A"}}},"comments":[{"texts":[{"value":"This heat stable bacteriocin shows activity against species of Lactobacillus, Listeria monocytogenes, Pediococcus, Enterococcus, Leuconostoc and Lactococcus"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacteriocin class IIA/YGNGV family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Bacteriocin bavaricin-A","featureId":"PRO_0000110573"},{"type":"Sequence uncertainty","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"K or D"},{"type":"Sequence uncertainty","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"G or N"}],"keywords":[{"id":"KW-0044","category":"Molecular function","name":"Antibiotic"},{"id":"KW-0929","category":"Molecular function","name":"Antimicrobial"},{"id":"KW-0078","category":"Molecular function","name":"Bacteriocin"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"8407671","citationType":"journal article","authors":["Larsen A.G.","Vogensen F.K.","Josephsen J."],"citationCrossReferences":[{"database":"PubMed","id":"8407671"},{"database":"DOI","id":"10.1111/j.1365-2672.1993.tb02755.x"}],"title":"Antimicrobial activity of lactic acid bacteria isolated from sour doughs: purification and characterization of bavaricin A, a bacteriocin produced by Lactobacillus bavaricus MI401.","publicationDate":"1993","journal":"J. Appl. Bacteriol.","firstPage":"113","lastPage":"122","volume":"75"},"referencePositions":["PROTEIN SEQUENCE"],"referenceComments":[{"value":"Bavaricus / MI401","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"Gene3D","id":"1.20.5.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023388","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_dom_sf"}]}],"sequence":{"value":"KYYGNGVHXGKHSXTVDWGTAIGNIGNNAAANXATGXNAGG","length":41,"molWeight":4061,"crc64":"88D192671EC8BB70","md5":"2ABAC19DAADC3C2740DD521E481C39C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Peptide":1,"Sequence uncertainty":2},"uniParcId":"UPI00001267A5"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48841","uniProtkbId":"PEPD_LATSK","entryAudit":{"firstPublicDate":"2001-09-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":65,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Probable dipeptidase"},"ecNumbers":[{"value":"3.4.13.19"}]}},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48940"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:59869"},{"database":"ChEBI","id":"CHEBI:77460"}],"ecNumber":"3.4.13.19"}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase C69 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Probable dipeptidase","featureId":"PRO_0000220384"},{"type":"Active site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-0224","category":"Molecular function","name":"Dipeptidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0645","category":"Molecular function","name":"Protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CU85UFRJFDNNL","citationType":"submission","authors":["van den Berg D.J.C.","Toonen M.Y.","Robijn G.W.","Kamerling J.P.","Vliegenthart J.F.G.","van der Swaluw C.D.M.","Ledoboer A.M.","Verrips C.T."],"title":"Isolation, characterization, and disruption of the putative exopolysaccharide gene cluster from Lactobactillus sake 0-1.","publicationDate":"JUN-1996","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"CBS 532.92 / 0-1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X98238","properties":[{"key":"ProteinId","value":"CAA66893.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q48841","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48841","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"C69.001","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AANHFMI","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0070004","properties":[{"key":"GoTerm","value":"F:cysteine-type exopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016805","properties":[{"key":"GoTerm","value":"F:dipeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.60.60.10","properties":[{"key":"EntryName","value":"Penicillin V Acylase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR047804","properties":[{"key":"EntryName","value":"C69_dipept_A-like"}]},{"database":"InterPro","id":"IPR005322","properties":[{"key":"EntryName","value":"Peptidase_C69"}]},{"database":"NCBIfam","id":"NF033678","properties":[{"key":"EntryName","value":"C69_fam_dipept"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12994:SF17","properties":[{"key":"EntryName","value":"LD30995P"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12994","properties":[{"key":"EntryName","value":"SECERNIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03577","properties":[{"key":"EntryName","value":"Peptidase_C69"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDRIELSACTSMMVGKNASIDGSTMISRNEDRFYAIHPKRFFVQPAVHNRHETYVSKYNGLTMPLPEEGYRYTSTPNGDLSDGLNEEDGINEKNVALSATESVYANERVLAYDPLIKNGLAEDSMCSLVLPYINSAREGVKLMGDIVTKYGSAEGNGIQYSDENEVWYQEIVTGHHWVAAKIPDDCYAVAANQVAIENIDFNDPDNYMWSEGIQEFVSGNHLNPSETEWNFRKIFGTDTEKDRHYNTPRVWYAQRYLNPEIKQEPESSDLPFIRKANRKLSVEDVQYVLKSHYNETEYDPLGNGTEEQKTTYRAISLSRTQNSHICQIRNNVPDAVKGVQWLGFGVPTFCPHVPFFTNANDTDETYRELPEKMTLKNAYWLHEALAMIVESHYGAFKQADIDYQKALSEWARTKIAATDKAIENQADAVAFLTAQNHEIATHYNEATTDLLAQLVTEGTQLSKLTFVMDKNL","length":473,"molWeight":53703,"crc64":"0EE0380ABC907E10","md5":"EBB14313D197E3D6F9830367B1971C42"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1},"uniParcId":"UPI00001315DA"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O53088","uniProtkbId":"ARCA_LATSK","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-06-01","entryVersion":106,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Arginine deiminase"},"shortNames":[{"value":"ADI"}],"ecNumbers":[{"value":"3.5.3.6"}]},"alternativeNames":[{"fullName":{"value":"Arginine dihydrolase"},"shortNames":[{"value":"AD"}]}]},"genes":[{"geneName":{"value":"arcA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginine + H2O = L-citrulline + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19597"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:32682"},{"database":"ChEBI","id":"CHEBI:57743"}],"ecNumber":"3.5.3.6"}},{"texts":[{"value":"Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the arginine deiminase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Arginine deiminase","featureId":"PRO_0000182215"},{"type":"Active site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Amidino-cysteine intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0056","category":"Biological process","name":"Arginine metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"9696763","citationType":"journal article","authors":["Zuniga M.","Champomier-Verges M.-C.","Zagorec M.","Perez-Martinez G."],"citationCrossReferences":[{"database":"PubMed","id":"9696763"},{"database":"DOI","id":"10.1128/jb.180.16.4154-4159.1998"}],"title":"Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sakei.","publicationDate":"1998","journal":"J. Bacteriol.","firstPage":"4154","lastPage":"4159","volume":"180"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ001330","properties":[{"key":"ProteinId","value":"CAA04682.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46741","properties":[{"key":"EntryName","value":"T46741"}]},{"database":"AlphaFoldDB","id":"O53088","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O53088","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00254","properties":[{"key":"RectionId","value":"UER00364"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016990","properties":[{"key":"GoTerm","value":"F:arginine deiminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006527","properties":[{"key":"GoTerm","value":"P:L-arginine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.3930.10","properties":[{"key":"EntryName","value":"Arginine deiminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.75.10.10","properties":[{"key":"EntryName","value":"L-arginine/glycine Amidinotransferase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00242","properties":[{"key":"EntryName","value":"Arg_deiminase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003876","properties":[{"key":"EntryName","value":"Arg_deiminase"}]},{"database":"NCBIfam","id":"TIGR01078","properties":[{"key":"EntryName","value":"arcA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002381","properties":[{"key":"EntryName","value":"PRK01388.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47271","properties":[{"key":"EntryName","value":"ARGININE DEIMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47271:SF2","properties":[{"key":"EntryName","value":"ARGININE DEIMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02274","properties":[{"key":"EntryName","value":"ADI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006356","properties":[{"key":"EntryName","value":"Arg_deiminase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01466","properties":[{"key":"EntryName","value":"ARGDEIMINASE"}]},{"database":"SUPFAM","id":"SSF55909","properties":[{"key":"EntryName","value":"Pentein"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSPIHVNSEIGKLKTVLLKRPGKEVENITPDIMYRLLFDDIPYLPTIQKEHDQFAQTLRDNGVEVLYLENLAAEAIDAGDVKEAFLDKMLNESHIKSPQVQAALKDYLISMATLDMVEKIMAGVRTNEIDIKSKALIDVSADDDYPFYMDPMPNLYFTRDPAASMGDGLTINKMTFEARQRESMFMEVIMQHHPRFANQGAQVWRDRDHIDRMEGGDELILSDKVLAIGISQRTSAQSIEELAKVLFANHSGFEKILAIKIPHKHAMMHLDTVFTMIDYDKFTIHPGIQGAGGMVDTYILEPGNNDEIKITHQTDLEKVLRDALEVPELTLIPCGGGDAVVAPREQWNDGSNTLAIAPGVVVTYDRNYVSNENLRQYGIKVIEVPSSELSRGRGGPRCMSMPLVRRKT","length":409,"molWeight":45914,"crc64":"B2703702B3382DB5","md5":"E308A073EEE5471D1BE5E9736E8AE09D"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1},"uniParcId":"UPI000004CCBF"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O87776","uniProtkbId":"GRPE_LATSK","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-11-01","entryVersion":90,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"Protein GrpE"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"HSP-70 cofactor"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"grpE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01151"}],"value":"Belongs to the GrpE family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Protein GrpE","featureId":"PRO_0000113802"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-MLRI030E54D8","citationType":"submission","authors":["Schmidt G.","Hertel C.","Hammes W.P."],"title":"Cloning and sequence analysis of the dnaK operon of Lactobacillus sakei LTH681.","publicationDate":"JUL-1998","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH681","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006274","properties":[{"key":"ProteinId","value":"CAA06940.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_016265326.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP017931.1"}]},{"database":"AlphaFoldDB","id":"O87776","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O87776","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"57132141","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000774","properties":[{"key":"GoTerm","value":"F:adenyl-nucleotide exchange factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042803","properties":[{"key":"GoTerm","value":"F:protein homodimerization activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051087","properties":[{"key":"GoTerm","value":"F:protein-folding chaperone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006457","properties":[{"key":"GoTerm","value":"P:protein folding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00446","properties":[{"key":"EntryName","value":"GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.22.10:FF:000001","properties":[{"key":"EntryName","value":"Protein GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.20.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.22.10","properties":[{"key":"EntryName","value":"Head domain of nucleotide exchange factor GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01151","properties":[{"key":"EntryName","value":"GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000740","properties":[{"key":"EntryName","value":"GrpE"}]},{"database":"InterPro","id":"IPR013805","properties":[{"key":"EntryName","value":"GrpE_CC"}]},{"database":"InterPro","id":"IPR009012","properties":[{"key":"EntryName","value":"GrpE_head"}]},{"database":"NCBIfam","id":"NF010738","properties":[{"key":"EntryName","value":"grpE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010759","properties":[{"key":"EntryName","value":"grpE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21237","properties":[{"key":"EntryName","value":"GRPE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21237:SF23","properties":[{"key":"EntryName","value":"GRPE PROTEIN HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01025","properties":[{"key":"EntryName","value":"GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00773","properties":[{"key":"EntryName","value":"GRPEPROTEIN"}]},{"database":"SUPFAM","id":"SSF58014","properties":[{"key":"EntryName","value":"Coiled-coil domain of nucleotide exchange factor GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51064","properties":[{"key":"EntryName","value":"Head domain of nucleotide exchange factor GrpE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01071","properties":[{"key":"EntryName","value":"GRPE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKQEKAENQEKPTEETVEETPKKETPFEPVMEADEVEETTEAQAPVEEADDKLAELQKKYDAMEDSFLRSQAEIKNIQMRNQKEQANLLKYDGQSLAKDVLPVLDNLERALAAEATDESLKKGVQMTYDHMKHALEDHGVKEIEAQGQAFDPTIHQAVQTVAVDGDQKADTVVQVFQKGYYLKDRVLRPAMVVVAQ","length":197,"molWeight":22247,"crc64":"F906543E2273AFB3","md5":"6A81AC55F6E87142B94BD2CAE5FAA004"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":2},"uniParcId":"UPI000012BB28"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O53090","uniProtkbId":"ARCC_LATSK","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":108,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Carbamate kinase"},"ecNumbers":[{"value":"2.7.2.2"}]}},"genes":[{"geneName":{"value":"arcC"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + ATP = carbamoyl phosphate + ADP + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10152"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.2"}},{"texts":[{"value":"Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the carbamate kinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"Carbamate kinase","featureId":"PRO_0000185127"}],"keywords":[{"id":"KW-0056","category":"Biological process","name":"Arginine metabolism"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9696763","citationType":"journal article","authors":["Zuniga M.","Champomier-Verges M.-C.","Zagorec M.","Perez-Martinez G."],"citationCrossReferences":[{"database":"PubMed","id":"9696763"},{"database":"DOI","id":"10.1128/jb.180.16.4154-4159.1998"}],"title":"Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sakei.","publicationDate":"1998","journal":"J. Bacteriol.","firstPage":"4154","lastPage":"4159","volume":"180"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ001330","properties":[{"key":"ProteinId","value":"CAA04684.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46743","properties":[{"key":"EntryName","value":"T46743"}]},{"database":"AlphaFoldDB","id":"O53090","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O53090","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AACNFAE","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"UniPathway","id":"UPA00996","properties":[{"key":"RectionId","value":"UER00366"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008804","properties":[{"key":"GoTerm","value":"F:carbamate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006525","properties":[{"key":"GoTerm","value":"P:arginine metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd04235","properties":[{"key":"EntryName","value":"AAK_CK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000007","properties":[{"key":"EntryName","value":"Carbamate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR003964","properties":[{"key":"EntryName","value":"Carb_kinase"}]},{"database":"NCBIfam","id":"TIGR00746","properties":[{"key":"EntryName","value":"arcC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009007","properties":[{"key":"EntryName","value":"PRK12352.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30409","properties":[{"key":"EntryName","value":"CARBAMATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30409:SF1","properties":[{"key":"EntryName","value":"CARBAMATE KINASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000723","properties":[{"key":"EntryName","value":"Carbamate_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01469","properties":[{"key":"EntryName","value":"CARBMTKINASE"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKRKIVVALGGNAILSTDASANAQIKAVKETVKQLVAFVKQGDQLIISHGNGPQVGNLLIQQAASDSEKTPAMPLDTVGAMSQGEIGYWMQNAFNEVLAEEGLALDVATIVTQTIVDAKDEAFQNPTKPIGPFYSEAEAKKQQSINPEAHFVEDAGRGWRRVVPSPRPIGIQEAPVIQKLVEGNVITISAGGGGVPVAKEGNKLRGVEAVIDKDFASEKLAELVGADMLIILTAVDNVYVNFNKPDQKKLTNVSVAELEDYIKDDQFAKGSMLPKIQTAIEYVNNRPDSKAIITSLDNVKNLLAHDAGTIITK","length":314,"molWeight":33652,"crc64":"7B717D56473A7FD8","md5":"954985159391C701458D4985F6897708"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI0000125DA6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A310","secondaryAccessions":["P35619","P80097"],"uniProtkbId":"SAKA_LATSK","entryAudit":{"firstPublicDate":"2005-03-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2005-03-15","entryVersion":71,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Bacteriocin sakacin-A"}},"flag":"Precursor"},"genes":[{"geneName":{"value":"sapA"},"synonyms":[{"value":"sakA"}]}],"comments":[{"texts":[{"value":"Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacteriocin class IIA/YGNGV family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Propeptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureId":"PRO_0000002749"},{"type":"Chain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Bacteriocin sakacin-A","featureId":"PRO_0000002750"},{"type":"Disulfide bond","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Beta strand","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XNO"}]},{"type":"Beta strand","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XNO"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XNO"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0044","category":"Molecular function","name":"Antibiotic"},{"id":"KW-0929","category":"Molecular function","name":"Antimicrobial"},{"id":"KW-0078","category":"Molecular function","name":"Bacteriocin"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"1487735","citationType":"journal article","authors":["Holck A.L.","Axelsson L.","Birkeland S.-E.","Aukrust T.","Blom H."],"citationCrossReferences":[{"database":"PubMed","id":"1487735"},{"database":"DOI","id":"10.1099/00221287-138-12-2715"}],"title":"Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706.","publicationDate":"1992","journal":"J. Gen. Microbiol.","firstPage":"2715","lastPage":"2720","volume":"138"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE"],"referenceComments":[{"value":"Lb706","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"7721704","citationType":"journal article","authors":["Axelsson L.","Holck A."],"citationCrossReferences":[{"database":"PubMed","id":"7721704"},{"database":"DOI","id":"10.1128/jb.177.8.2125-2137.1995"}],"title":"The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706.","publicationDate":"1995","journal":"J. Bacteriol.","firstPage":"2125","lastPage":"2137","volume":"177"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"Lb706","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Z14233","properties":[{"key":"ProteinId","value":"CAA78600.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"Z46867","properties":[{"key":"ProteinId","value":"CAA86942.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"C56273","properties":[{"key":"EntryName","value":"C56273"}]},{"database":"RefSeq","id":"WP_032488606.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAHIAI010000055.1"}]},{"database":"PDB","id":"7XNO","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"2.54 A"},{"key":"Chains","value":"A/C/G=19-59"}]},{"database":"AlphaFoldDB","id":"P0A310","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-33321","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0A310","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"1.C.24.1.8","properties":[{"key":"FamilyName","value":"the pediocin (pediocin) family"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0042742","properties":[{"key":"GoTerm","value":"P:defense response to bacterium"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.20.5.130:FF:000001","properties":[{"key":"EntryName","value":"Bacteriocin hiracin-JM79"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002633","properties":[{"key":"EntryName","value":"Bacteriocin_IIa"}]},{"database":"InterPro","id":"IPR023384","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_CS"}]},{"database":"InterPro","id":"IPR023388","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_dom_sf"}]},{"database":"InterPro","id":"IPR010133","properties":[{"key":"EntryName","value":"Bacteriocin_signal_seq"}]},{"database":"NCBIfam","id":"TIGR01847","properties":[{"key":"EntryName","value":"bacteriocin_sig"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01721","properties":[{"key":"EntryName","value":"Bacteriocin_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS60030","properties":[{"key":"EntryName","value":"BACTERIOCIN_IIA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNNVKELSMTELQTITGGARSYGNGVYCNNKKCWVNRGEATQSIIGGMISGWASGLAGM","length":59,"molWeight":6257,"crc64":"CEE4B0EB5470574A","md5":"5CF56483E42DA235FFA6F0CE3AD9BF02"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Propeptide":1,"Chain":1,"Disulfide bond":1,"Beta strand":2,"Helix":1},"uniParcId":"UPI000013551F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48838","uniProtkbId":"SDHA_LATSK","entryAudit":{"firstPublicDate":"1999-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":72,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Probable L-serine dehydratase, alpha chain"},"shortNames":[{"value":"SDH"}],"ecNumbers":[{"value":"4.3.1.17"}]},"alternativeNames":[{"fullName":{"value":"L-serine deaminase"},"shortNames":[{"value":"L-SD"}]}],"flag":"Fragment"},"genes":[{"geneName":{"value":"sdhA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-serine = pyruvate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19169"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:33384"}],"ecNumber":"4.3.1.17"}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Heterodimer of an alpha chain and a beta chain"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the iron-sulfur dependent L-serine dehydratase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"OUTSIDE"},"end":{"value":209,"modifier":"EXACT"}},"description":"Probable L-serine dehydratase, alpha chain","featureId":"PRO_0000171914"},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CU85UFRJFDNNL","citationType":"submission","authors":["van den Berg D.J.C.","Toonen M.Y.","Robijn G.W.","Kamerling J.P.","Vliegenthart J.F.G.","van der Swaluw C.D.M.","Ledoboer A.M.","Verrips C.T."],"title":"Isolation, characterization, and disruption of the putative exopolysaccharide gene cluster from Lactobactillus sake 0-1.","publicationDate":"JUN-1996","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"CBS 532.92 / 0-1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X98238","properties":[{"key":"ProteinId","value":"CAA66890.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q48838","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48838","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AASMCGM","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"UniPathway","id":"UPA00138","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0003941","properties":[{"key":"GoTerm","value":"F:L-serine ammonia-lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"InterPro","id":"IPR051318","properties":[{"key":"EntryName","value":"Fe-S_L-Ser"}]},{"database":"InterPro","id":"IPR005130","properties":[{"key":"EntryName","value":"Ser_deHydtase-like_asu"}]},{"database":"InterPro","id":"IPR004642","properties":[{"key":"EntryName","value":"Ser_deHydtase_asu"}]},{"database":"NCBIfam","id":"TIGR00718","properties":[{"key":"EntryName","value":"sda_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30182","properties":[{"key":"EntryName","value":"L-SERINE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30182:SF1","properties":[{"key":"EntryName","value":"L-SERINE DEHYDRATASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03313","properties":[{"key":"EntryName","value":"SDH_alpha"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"DIMLEAVQNAIATNEVNASMGIICATPTAGSAGTLPGILSVITKQLSLDRDAQIRFLFCASAFGMVVANDAMIAGATGGCQAEVGSASAMGAAAAVEAAGGTHQQSSEAFAMAMSNLLGLVCDPVAGLVEVPCVKRNVIGSVNALTSADMALAGLVSKIPADEVISAMKSIGENLPSTLRETGLGGLAATPTGIALKMQIFGQDMSIDK","length":209,"molWeight":20887,"crc64":"D180E92BD55670BF","md5":"2A88D95ECB0B2B3FD4CAC6167E806738"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":1},"uniParcId":"UPI0000135724"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48847","uniProtkbId":"BGAM_LATSK","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":82,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Beta-galactosidase small subunit"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Beta-gal small subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q02604"}],"value":"3.2.1.23"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8574399"}],"value":"lacM"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8574399"}],"value":"Component of a beta-galactosidase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.","ecNumber":"3.2.1.23","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q02604"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8574399"}],"value":"Heterodimer of a large (LacL) and a small subunit (LacM)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacterial beta-galactosidase small subunit family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Beta-galactosidase small subunit","featureId":"PRO_0000057671"}],"keywords":[{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"8574399","citationType":"journal article","authors":["Obst M.","Meding E.R.","Vogel R.F.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"8574399"},{"database":"DOI","id":"10.1099/13500872-141-12-3059"}],"title":"Two genes encoding the beta-galactosidase of Lactobacillus sake.","publicationDate":"1995","journal":"Microbiology","firstPage":"3059","lastPage":"3066","volume":"141"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","SUBUNIT"],"referenceComments":[{"value":"ATCC 15521 / DSM 20017 / JCM 1157 / CCUG 30501 / CIP 103139 / KCTC 3603 / NBRC 15893 / NCIMB 13090 / T.S","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X82287","properties":[{"key":"ProteinId","value":"CAA57731.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_025015979.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CEMAWX010000007.1"}]},{"database":"AlphaFoldDB","id":"Q48847","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48847","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH2","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 2"}]},{"database":"OMA","id":"ADMFTKC","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0009341","properties":[{"key":"GoTerm","value":"C:beta-galactosidase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004565","properties":[{"key":"GoTerm","value":"F:beta-galactosidase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005990","properties":[{"key":"GoTerm","value":"P:lactose catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"2.70.98.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004199","properties":[{"key":"EntryName","value":"B-gal_small/dom_5"}]},{"database":"InterPro","id":"IPR050347","properties":[{"key":"EntryName","value":"Bact_Beta-galactosidase"}]},{"database":"InterPro","id":"IPR011013","properties":[{"key":"EntryName","value":"Gal_mutarotase_sf_dom"}]},{"database":"InterPro","id":"IPR014718","properties":[{"key":"EntryName","value":"GH-type_carb-bd"}]},{"database":"PANTHER","id":"PTHR46323","properties":[{"key":"EntryName","value":"BETA-GALACTOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46323:SF2","properties":[{"key":"EntryName","value":"BETA-GALACTOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02929","properties":[{"key":"EntryName","value":"Bgal_small_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01038","properties":[{"key":"EntryName","value":"Bgal_small_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF74650","properties":[{"key":"EntryName","value":"Galactose mutarotase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANTNKRLAVIFGDVTLGLKGPDFHYLFSYQTGGPESLRIQGKEWLYRSPKPTFWRATTDNDRGNQFPLKSGMWLAADQFIACQSITVAIDGQTIPLPIAPENNRYSGRETAQEVTVTYTYQTITTPQTTVEVSYTIQASGKIRVAVTYHGQAGLPSLPVFGLRFVMPTPATRFIYQGLSGETYPDRMAGGIAGEYEVTGLPVTPYLVPQDCGVHMATDWVTIYRQAVLDNCLHEPVETGLKFKMVDQPFAFSCLPYTAEELENATHHSELPAPHRTVLNLLGAVRGVGGIDSWGSDVEVAYQIDATQDRHFEFEISF","length":318,"molWeight":35254,"crc64":"6F55CDB90F67FC75","md5":"BB50FE4FE1C92E6E69B1E1CAAC145960"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00001268F4"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O87777","uniProtkbId":"DNAK_LATSK","entryAudit":{"firstPublicDate":"2001-04-27","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-11-01","entryVersion":109,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"value":"Chaperone protein DnaK"}},"alternativeNames":[{"fullName":{"value":"HSP70"}},{"fullName":{"value":"Heat shock 70 kDa protein"}},{"fullName":{"value":"Heat shock protein 70"}}]},"genes":[{"geneName":{"value":"dnaK"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Acts as a chaperone"}],"commentType":"FUNCTION"},{"texts":[{"value":"By heat shock as well as salt or ethanol stress"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the heat shock protein 70 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Chaperone protein DnaK","featureId":"PRO_0000078476"},{"type":"Region","location":{"start":{"value":577,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"10553284","citationType":"journal article","authors":["Schmidt G.","Hertel C.","Hammes W.P."],"citationCrossReferences":[{"database":"PubMed","id":"10553284"},{"database":"DOI","id":"10.1016/s0723-2020(99)80039-3"}],"title":"Molecular characterisation of the dnaK operon of Lactobacillus sakei LTH681.","publicationDate":"1999","journal":"Syst. Appl. Microbiol.","firstPage":"321","lastPage":"328","volume":"22"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH681","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006274","properties":[{"key":"ProteinId","value":"CAA06941.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_016265325.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BJLN01000010.1"}]},{"database":"AlphaFoldDB","id":"O87777","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O87777","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"57132140","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006457","properties":[{"key":"GoTerm","value":"P:protein folding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd10234","properties":[{"key":"EntryName","value":"ASKHA_NBD_HSP70_DnaK-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.34.10:FF:000014","properties":[{"key":"EntryName","value":"Chaperone protein DnaK HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000071","properties":[{"key":"EntryName","value":"Molecular chaperone DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.640.10:FF:000003","properties":[{"key":"EntryName","value":"Molecular chaperone DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.640.10","properties":[{"key":"EntryName","value":"Actin, Chain A, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.34.10","properties":[{"key":"EntryName","value":"Substrate Binding Domain Of DNAk, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00332","properties":[{"key":"EntryName","value":"DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR012725","properties":[{"key":"EntryName","value":"Chaperone_DnaK"}]},{"database":"InterPro","id":"IPR018181","properties":[{"key":"EntryName","value":"Heat_shock_70_CS"}]},{"database":"InterPro","id":"IPR029048","properties":[{"key":"EntryName","value":"HSP70_C_sf"}]},{"database":"InterPro","id":"IPR029047","properties":[{"key":"EntryName","value":"HSP70_peptide-bd_sf"}]},{"database":"InterPro","id":"IPR013126","properties":[{"key":"EntryName","value":"Hsp_70_fam"}]},{"database":"NCBIfam","id":"NF001413","properties":[{"key":"EntryName","value":"dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02350","properties":[{"key":"EntryName","value":"prok_dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19375","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 70KDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00012","properties":[{"key":"EntryName","value":"HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00301","properties":[{"key":"EntryName","value":"HEATSHOCK70"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF100934","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100920","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00297","properties":[{"key":"EntryName","value":"HSP70_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00329","properties":[{"key":"EntryName","value":"HSP70_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01036","properties":[{"key":"EntryName","value":"HSP70_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKVIGIDLGTTNSAVAVLEGGQPKIITNPEGARTTPSVVSFKNGEIQVGEVAKRQAITNPDTIASIKRHIGEAGYKVTVGDKSYTPQEVSAMILQYIKKFAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGKIAGLDVKRIINEPTASALAYGLDKTETDEKVLVYDLGGGTFDVSVLELGDGVFQVLSTNGDTRLGGDDFDEAIMNWLVENFKSDNGIDLSKDKMAMQRLKDAAEKAKKDLSGVSSTQISLPFISAGENGPLHLEMTLSRTEFDRLTSDLVDRTKAPVMNALKDAGLDANEIDKVILNGGSTRIPAVQEAVKNWTGKEPDHSINPDEAVALGAAVQGGVISGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKAQTFSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPAAPRGVPQIEVKFDIDKNGIVNVSAKDLGTNKEQKITIKSNSGLSDEEIDRMMKEAQENEEADTKRKEEVDLKNDVDQLIFQTDKTLKELEGKVSDEELQKAKDAKEELVKAQQENNLEDMKTKRDALSEIVQELTVKLYQQAQEAQQAAGGAEGNATDAKTDDGTVDGDFEEVKDDKE","length":613,"molWeight":66276,"crc64":"1D9348482479A64F","md5":"5365FBFA40910A80A6DAB76DA8C71B72"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":1,"Modified residue":1},"uniParcId":"UPI00001295D3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P80493","uniProtkbId":"BAVM_LATSK","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-07-15","entryVersion":65,"sequenceVersion":2},"annotationScore":2.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Bacteriocin bavaricin-MN"}}},"comments":[{"texts":[{"value":"Has antimicrobial activity"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacteriocin class IIA/YGNGV family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Bacteriocin bavaricin-MN","featureId":"PRO_0000110574"},{"type":"Disulfide bond","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Sequence uncertainty","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":""},{"type":"Sequence uncertainty","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0044","category":"Molecular function","name":"Antibiotic"},{"id":"KW-0929","category":"Molecular function","name":"Antimicrobial"},{"id":"KW-0078","category":"Molecular function","name":"Bacteriocin"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"8953724","citationType":"journal article","authors":["Kaiser A.L.","Montville T.J."],"citationCrossReferences":[{"database":"PubMed","id":"8953724"},{"database":"DOI","id":"10.1128/aem.62.12.4529-4535.1996"}],"title":"Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles.","publicationDate":"1996","journal":"Appl. Environ. Microbiol.","firstPage":"4529","lastPage":"4535","volume":"62"},"referencePositions":["PROTEIN SEQUENCE"],"referenceComments":[{"value":"MN","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"TCDB","id":"1.C.24.1.9","properties":[{"key":"FamilyName","value":"the pediocin (pediocin) family"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0042742","properties":[{"key":"GoTerm","value":"P:defense response to bacterium"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.5.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002633","properties":[{"key":"EntryName","value":"Bacteriocin_IIa"}]},{"database":"InterPro","id":"IPR023384","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_CS"}]},{"database":"InterPro","id":"IPR023388","properties":[{"key":"EntryName","value":"Bacteriocin_IIa_dom_sf"}]},{"database":"Pfam","id":"PF01721","properties":[{"key":"EntryName","value":"Bacteriocin_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS60030","properties":[{"key":"EntryName","value":"BACTERIOCIN_IIA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"TKYYGNGVYCNSKKCWVDWGQAAGGIGQTVVXGWLGGAIPGK","length":42,"molWeight":4402,"crc64":"0E6282C934C04F02","md5":"483F42C2ECF6E9F03DE4B2795ED53485"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Peptide":1,"Disulfide bond":1,"Sequence uncertainty":2},"uniParcId":"UPI00001267A6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O87775","uniProtkbId":"HRCA_LATSK","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-11-01","entryVersion":96,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00081"}],"value":"Heat-inducible transcription repressor HrcA"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00081"}],"value":"hrcA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00081"}],"value":"Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00081"}],"value":"Belongs to the HrcA family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Heat-inducible transcription repressor HrcA","featureId":"PRO_0000182490"}],"keywords":[{"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"id":"KW-0346","category":"Biological process","name":"Stress response"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-MLRI030E54D8","citationType":"submission","authors":["Schmidt G.","Hertel C.","Hammes W.P."],"title":"Cloning and sequence analysis of the dnaK operon of Lactobacillus sakei LTH681.","publicationDate":"JUL-1998","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"LTH681","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006274","properties":[{"key":"ProteinId","value":"CAA06939.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_016265327.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_MKDM01000011.1"}]},{"database":"AlphaFoldDB","id":"O87775","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O87775","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0045892","properties":[{"key":"GoTerm","value":"P:negative regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.450.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.390.60","properties":[{"key":"EntryName","value":"Heat-inducible transcription repressor hrca homolog, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00081","properties":[{"key":"EntryName","value":"HrcA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029016","properties":[{"key":"EntryName","value":"GAF-like_dom_sf"}]},{"database":"InterPro","id":"IPR002571","properties":[{"key":"EntryName","value":"HrcA"}]},{"database":"InterPro","id":"IPR021153","properties":[{"key":"EntryName","value":"HrcA_C"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR036390","properties":[{"key":"EntryName","value":"WH_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR005104","properties":[{"key":"EntryName","value":"WHTH_HrcA_DNA-bd"}]},{"database":"InterPro","id":"IPR023120","properties":[{"key":"EntryName","value":"WHTH_transcript_rep_HrcA_IDD"}]},{"database":"NCBIfam","id":"TIGR00331","properties":[{"key":"EntryName","value":"hrcA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34824","properties":[{"key":"EntryName","value":"HEAT-INDUCIBLE TRANSCRIPTION REPRESSOR HRCA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34824:SF1","properties":[{"key":"EntryName","value":"HEAT-INDUCIBLE TRANSCRIPTION REPRESSOR HRCA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01628","properties":[{"key":"EntryName","value":"HrcA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03444","properties":[{"key":"EntryName","value":"WHD_HrcA"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005485","properties":[{"key":"EntryName","value":"HrcA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55781","properties":[{"key":"EntryName","value":"GAF domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46785","properties":[{"key":"EntryName","value":"Winged helix' DNA-binding domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLTERQLMILKEIIRLFTESGQPVGSKKLMSELPMHVSSATIRNDMADLENVGLIEKTHSSSGRVPSMKGYRYYLDHLIQPAVLNPMDVATVQQSFGRHYHKIDEIVSQSANILSNLTSYTAITLGPEMAEIRLTGFRLVPLGNHQVMAIIVTSAGTVDNQVFTIPNAISGDELEKAIRVVNDHLIGLPLTVVSQKLKTEVPALLMQYMGSPGGFLNIFDDVLKQASQERLYVGGQSNLLNFSELTDVSQLKSIYNIINQSDDLAKLLELSPGEANSQVQVRLGDEMTNDLLKNYSLMTVNYDVGEHGQGLIALLGPTSMPHSRMIGLLDLFREELAKKLIDYYADFDDNQS","length":352,"molWeight":39011,"crc64":"9E2A289AED68C7AB","md5":"725B43666E660097EE665AC58D9DF6A1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI000012CB9C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O07127","uniProtkbId":"YPTY_LATSK","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1997-07-01","entryVersion":83,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Uncharacterized 16.5 kDa protein in ptsI 3'region"}},"alternativeNames":[{"fullName":{"value":"ORFY"}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the BlaI transcriptional regulatory family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Uncharacterized 16.5 kDa protein in ptsI 3'region","featureId":"PRO_0000062801"}],"keywords":[{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"9172326","citationType":"journal article","authors":["Stentz R.","Lauret R.","Ehrlich S.D.","Morel-Deville F.","Zagorec M."],"citationCrossReferences":[{"database":"PubMed","id":"9172326"},{"database":"DOI","id":"10.1128/aem.63.6.2111-2116.1997"}],"title":"Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"2111","lastPage":"2116","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"160*1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U82366","properties":[{"key":"ProteinId","value":"AAC45392.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O07127","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O07127","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"AAEWQVM","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0045892","properties":[{"key":"GoTerm","value":"P:negative regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005650","properties":[{"key":"EntryName","value":"BlaI_family"}]},{"database":"InterPro","id":"IPR014071","properties":[{"key":"EntryName","value":"Cu_transp_CopY/TcrY"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR036390","properties":[{"key":"EntryName","value":"WH_DNA-bd_sf"}]},{"database":"NCBIfam","id":"TIGR02698","properties":[{"key":"EntryName","value":"CopY_TcrY"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03965","properties":[{"key":"EntryName","value":"Penicillinase_R"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF019455","properties":[{"key":"EntryName","value":"CopR_AtkY"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46785","properties":[{"key":"EntryName","value":"Winged helix' DNA-binding domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAENTNEITTSEWEVMRIVWSLGQVNSRDLIDLLQPKRDWQDSTIKTLIGRLVKKGFLKTEKEGRRFNYTATVPEIEAMENATQSLFEHLCGMKKGQTLAALIDQTTLSQTDILQLQQLLTAKAATAPEKVACDCLPNKCDCEKEE","length":146,"molWeight":16504,"crc64":"A444B60BFC6BD968","md5":"932370DC6960D0D41E4FEB5CF1DAEDD2"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI0000000919"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48864","uniProtkbId":"SAIA_LATSK","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":51,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Sakacin-A immunity factor"}}},"genes":[{"geneName":{"value":"saiA"}}],"comments":[{"texts":[{"value":"Imparts immunity to sakacin-A to naturally sensitive host strains"}],"commentType":"FUNCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Sakacin-A immunity factor","featureId":"PRO_0000206202"},{"type":"Helix","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]},{"type":"Helix","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]},{"type":"Helix","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]},{"type":"Helix","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]},{"type":"Turn","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]},{"type":"Helix","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7XTG"}]}],"geneLocations":[{"value":"60 kb","geneEncodingType":"Plasmid"}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0079","category":"Biological process","name":"Bacteriocin immunity"},{"id":"KW-0614","category":"Technical term","name":"Plasmid"}],"references":[{"referenceNumber":1,"citation":{"id":"7721704","citationType":"journal article","authors":["Axelsson L.","Holck A."],"citationCrossReferences":[{"database":"PubMed","id":"7721704"},{"database":"DOI","id":"10.1128/jb.177.8.2125-2137.1995"}],"title":"The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706.","publicationDate":"1995","journal":"J. Bacteriol.","firstPage":"2125","lastPage":"2137","volume":"177"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"Lb706","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Z46867","properties":[{"key":"ProteinId","value":"CAA86941.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"B56273","properties":[{"key":"EntryName","value":"B56273"}]},{"database":"RefSeq","id":"WP_076981511.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAHIAC010000059.1"}]},{"database":"PDB","id":"7XNO","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"2.54 A"},{"key":"Chains","value":"B/F/J=1-90"}]},{"database":"PDB","id":"7XTG","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"B/F/J=3-90"}]},{"database":"AlphaFoldDB","id":"Q48864","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-33321","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-33448","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48864","properties":[{"key":"Description","value":"-"}]},{"database":"SUPFAM","id":"SSF109797","properties":[{"key":"EntryName","value":"Bacteriocin immunity protein-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKADYKKINSILTYTSTALKNPKIIKDKDLVVLLTIIQEEAKQNRIFYDYKRKFRPAVTRFTIDNNFEIPDCLVKLLSAVETPKAWSGFS","length":90,"molWeight":10458,"crc64":"DE9689A2AA18AA1F","md5":"B20A74671EB106E848697DB972FE10A1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1},"countByFeatureType":{"Chain":1,"Helix":5,"Turn":1},"uniParcId":"UPI000013551D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q5QGJ0","uniProtkbId":"Q5QGJ0_LATSK","entryAudit":{"firstPublicDate":"2005-01-04","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2005-01-04","entryVersion":119,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Latilactobacillus sakei","commonName":"Lactobacillus sakei","taxonId":1599,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAU85377.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Latilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAU85377.1"}],"value":"pfk"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKX76612.1"}],"value":"pfkA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKX76612.1"}],"value":"CUR37_08940"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WGI18308.1"}],"value":"QBD03_05990"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"15574925","citationType":"journal article","authors":["Marceau A.","Zagorec M.","Chaillou S.","Mera T.","Champomier-Verges M.C."],"citationCrossReferences":[{"database":"PubMed","id":"15574925"},{"database":"DOI","id":"10.1128/AEM.70.12.7260-7268.2004"}],"title":"Evidence for involvement of at least six proteins in adaptation of Lactobacillus sakei to cold temperatures and addition of NaCl.","publicationDate":"2004","journal":"Appl. Environ. Microbiol.","firstPage":"7260","lastPage":"7268","volume":"70"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAU85377.1"}]},{"referenceNumber":2,"citation":{"id":"CI-AAL8MJCIMQB90","citationType":"submission","authors":["Champomier Verges M.C.","Marceau A.","Chaillou S.P.","Zagorec M."],"publicationDate":"APR-2004","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAU85377.1"}]},{"referenceNumber":3,"citation":{"id":"CI-8I2BH8BL2MB3V","citationType":"submission","authors":["Inglin R.C."],"publicationDate":"SEP-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKX76612.1"}],"value":"RI-517","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"PKX76612.1"}]},{"referenceNumber":4,"citation":{"id":"CI-F877I15QFUJD","citationType":"submission","authors":["Kim S.Y."],"title":"Novel strain of Lactilactobacillus sakei and use thereof.","publicationDate":"APR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WGI18308.1"}],"value":"HUP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"WGI18308.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY588237","properties":[{"key":"ProteinId","value":"AAU85377.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MKGH01000044","properties":[{"key":"ProteinId","value":"PKX76612.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"CP122959","properties":[{"key":"ProteinId","value":"WGI18308.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_011374735.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BJLN01000001.1"}]},{"database":"AlphaFoldDB","id":"Q5QGJ0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"57133891","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1599.17.peg.511","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRIGILTSGGDAPGMNAAVRAVARKAMHEGLEVYGINYGYAGLVAGDIFKMDPITVGDKIQRGGTFLYSARYPEFAQVEGQLKGIEQLNKFGIEALVVIGGDGSYHGALRLTEHGYNAIGLPGTIDNDIPFTDQTIGFDTAVNTVLESIDRIRDTAASHERTFVVEVMGRGAGDIALWAGVAGGAQDIIIPERDFDVKAVAEKLRASREHGQKHAIIVLAEGVMHADEFSEKLSEYGDFHLRSTVLGHVVRGGSPTASDRVLASRLGSKAVELLLEGKGGVALGIEKNEIIAHDMLDLFNHKHHAMLDLYDLNEDLAY","length":319,"molWeight":34350,"crc64":"28A3E214BCE51B4B","md5":"8C5CD416A47A1FEF22CC5CF9A6252624"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":12},"uniParcId":"UPI0000497ED4"}}]}