{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q9LCK8","uniProtkbId":"Q9LCK8_9PORP","entryAudit":{"firstPublicDate":"2000-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-10-01","entryVersion":123,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Porphyromonas asaccharolytica","taxonId":28123,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019166"}],"value":"DNA gyrase subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012895"}],"value":"5.6.2.2"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}],"value":"gyrB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001978"}],"value":"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000185"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011234"}],"value":"Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010708"}],"value":"Belongs to the type II topoisomerase GyrB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Site","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":553,"modifier":"EXACT"},"end":{"value":553,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"10555336","citationType":"journal article","authors":["Suzuki M.","Nakagawa Y.","Harayama S.","Yamamoto S."],"citationCrossReferences":[{"database":"PubMed","id":"10555336"}],"title":"Phylogenetic analysis of genus Marinilabilia and related bacteria based on the amino acid sequences of GyrB and amended description of Marinilabilia salmonicolor with Marinilabilia agarovorans as its subjective synonym.","publicationDate":"1999","journal":"Int. J. Syst. Bacteriol.","firstPage":"1551","lastPage":"1557","volume":"49"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}],"value":"JCM 6326","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAA90679.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB015030","properties":[{"key":"ProteinId","value":"BAA90679.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9LCK8","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:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003918","properties":[{"key":"GoTerm","value":"F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16928","properties":[{"key":"EntryName","value":"HATPase_GyrB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00822","properties":[{"key":"EntryName","value":"TopoII_Trans_DNA_gyrase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03366","properties":[{"key":"EntryName","value":"TOPRIM_TopoIIA_GyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000005","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.670:FF:000001","properties":[{"key":"EntryName","value":"DNA topoisomerase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.670","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"InterPro","id":"IPR001241","properties":[{"key":"EntryName","value":"Topo_IIA"}]},{"database":"InterPro","id":"IPR013760","properties":[{"key":"EntryName","value":"Topo_IIA-like_dom_sf"}]},{"database":"InterPro","id":"IPR000565","properties":[{"key":"EntryName","value":"Topo_IIA_B"}]},{"database":"InterPro","id":"IPR013759","properties":[{"key":"EntryName","value":"Topo_IIA_B_C"}]},{"database":"InterPro","id":"IPR013506","properties":[{"key":"EntryName","value":"Topo_IIA_bsu_dom2"}]},{"database":"InterPro","id":"IPR018522","properties":[{"key":"EntryName","value":"TopoIIA_CS"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"InterPro","id":"IPR034160","properties":[{"key":"EntryName","value":"TOPRIM_GyrB"}]},{"database":"NCBIfam","id":"NF004189","properties":[{"key":"EntryName","value":"PRK05644.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011501","properties":[{"key":"EntryName","value":"PRK14939.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866:SF1","properties":[{"key":"EntryName","value":"DNA GYRASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00204","properties":[{"key":"EntryName","value":"DNA_gyraseB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02518","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01751","properties":[{"key":"EntryName","value":"Toprim"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01159","properties":[{"key":"EntryName","value":"DNAGYRASEB"}]},{"database":"PRINTS","id":"PR00418","properties":[{"key":"EntryName","value":"TPI2FAMILY"}]},{"database":"SMART","id":"SM00387","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00433","properties":[{"key":"EntryName","value":"TOP2c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56719","properties":[{"key":"EntryName","value":"Type II DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00177","properties":[{"key":"EntryName","value":"TOPOISOMERASE_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50880","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GDISEKGLHHLVYEVVDNSIDEALAGYCTEVLVEILSDNSIQVTDNGRGIPVDMHAKEGKSALEVVMTVLHAGGKFDKGSYKVSGGLHGVGVSCVNALSESLIAEVHRDGKIYRQEYSRGKPLTGVEVVGKADDTGTRITFKPDDTIFRETIYSSETLSHRLRELSYLNAGLHLKLIDHRVHDEEGQPKSWIFYSENGLSEFVRYVDGAKESLIHDVIHHTTEKQGVPVEVALTYNTSYQENVYTYVNDIHTIEGGTHLTGFRRGLTRTLKKYATDSHLLDKIKEEISGDDFREGLTAIVSVKVAEPQFEGQTKTKLGNSEIVGVVDAAVSEALEIYLEEHPTEAKLIVDKVILAAQARHAARRARELVQRKSPLTGGGLPGKLADCSSKDPSECELFIVEGDSAGGTAKQGRDSKYQAILPLRGKILNVEKAMQHRILDNAEIKNIYTALGVTVGTEEDSKALNLSKLRYHKIIIMTDADVDGAHIATLILTFFFRNMRPLIENGYVYIANPPLYLCKKDRIEEYCWTDEQKSDFVTKYGNGQENRIKIQRY","length":553,"molWeight":61465,"crc64":"89C0B62FC475DE13","md5":"E6C8F04E4C9DCD5C7FD8C8C9130F91A7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Site":2,"Non-terminal residue":2},"uniParcId":"UPI00000AF612"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D9N3F2","uniProtkbId":"D9N3F2_9PORP","entryAudit":{"firstPublicDate":"2010-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-10-05","entryVersion":42,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Porphyromonas asaccharolytica","taxonId":28123,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}],"value":"Heat shock protein 60"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}],"value":"hsp60"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006607"}],"value":"Belongs to the chaperonin (HSP60) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"20671088","citationType":"journal article","authors":["Sakamoto M.","Ohkuma M."],"citationCrossReferences":[{"database":"PubMed","id":"20671088"},{"database":"DOI","id":"10.1099/jmm.0.020420-0"}],"title":"Usefulness of the hsp60 gene for the identification and classification of Gram-negative anaerobic rods.","publicationDate":"2010","journal":"J. Med. Microbiol.","firstPage":"1293","lastPage":"1302","volume":"59"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}],"value":"JCM 6326","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAJ13405.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB547573","properties":[{"key":"ProteinId","value":"BAJ13405.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"D9N3F2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140662","properties":[{"key":"GoTerm","value":"F:ATP-dependent protein folding chaperone"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042026","properties":[{"key":"GoTerm","value":"P:protein refolding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.50.7.10:FF:000001","properties":[{"key":"EntryName","value":"60 kDa chaperonin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.7.10","properties":[{"key":"EntryName","value":"GroEL"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.260.10","properties":[{"key":"EntryName","value":"TCP-1-like chaperonin intermediate domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001844","properties":[{"key":"EntryName","value":"Cpn60/GroEL"}]},{"database":"InterPro","id":"IPR002423","properties":[{"key":"EntryName","value":"Cpn60/GroEL/TCP-1"}]},{"database":"InterPro","id":"IPR027409","properties":[{"key":"EntryName","value":"GroEL-like_apical_dom_sf"}]},{"database":"InterPro","id":"IPR027413","properties":[{"key":"EntryName","value":"GROEL-like_equatorial_sf"}]},{"database":"InterPro","id":"IPR027410","properties":[{"key":"EntryName","value":"TCP-1-like_intermed_sf"}]},{"database":"PANTHER","id":"PTHR45633","properties":[{"key":"EntryName","value":"60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00118","properties":[{"key":"EntryName","value":"Cpn60_TCP1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52029","properties":[{"key":"EntryName","value":"GroEL apical domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48592","properties":[{"key":"EntryName","value":"GroEL equatorial domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"ATVLAQSIINVGLKNITSGANPMEVKRGIDKAVKAVVESIRKQAKEVGDDLEQIAHVATISANGDEEIGQLIAQAMEKVKKEGVITVEEAKGIDTTVDIVEGMQFDNGYISPYFVTDPEKMECRMEKPYILFYEKKLSTIKDLLPLLEKVLQQGRSLLIIAEDIESEALTTLVLNRLRAGLKICGV","length":186,"molWeight":20415,"crc64":"303C49B995B937D1","md5":"AB60CCA370C07AC2C6311FA779AD2152"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Non-terminal residue":2},"uniParcId":"UPI0001DD3D18"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q69FX6","uniProtkbId":"Q69FX6_9PORP","entryAudit":{"firstPublicDate":"2004-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-09-13","entryVersion":62,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Porphyromonas asaccharolytica","taxonId":28123,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}],"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012418"}],"value":"DNA-directed RNA polymerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012418"}],"value":"2.7.7.6"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}],"value":"rpoB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000434"}],"value":"Belongs to the RNA polymerase beta chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"RNA polymerase Rpb2","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04565"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"17184287","citationType":"journal article","authors":["Ko K.S.","Kuwahara T.","Haehwa L.","Yoon Y.J.","Kim B.J.","Lee K.H.","Ohnishi Y.","Kook Y.H."],"citationCrossReferences":[{"database":"PubMed","id":"17184287"},{"database":"DOI","id":"10.1111/j.1469-0691.2006.01553.x"}],"title":"RNA polymerase beta-subunit gene (rpoB) sequence analysis for the identification of Bacteroides spp.","publicationDate":"2007","journal":"Clin. Microbiol. Infect.","firstPage":"48","lastPage":"54","volume":"13"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}],"value":"NCTC 9337","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR10402.1"}]},{"referenceNumber":2,"citation":{"id":"CI-FCRPAQB7D3VJS","citationType":"submission","authors":["Sakamoto M.","Ohkuma M."],"title":"Multilocus sequence analysis of the genus Bacteroides and related taxa.","publicationDate":"OCT-2014","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBA57025.1"}],"value":"JCM 6326","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBA57025.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY338190","properties":[{"key":"ProteinId","value":"AAR10402.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"LC005338","properties":[{"key":"ProteinId","value":"BBA57025.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q69FX6","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:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.1100.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015712","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_su2"}]},{"database":"InterPro","id":"IPR007645","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_3"}]},{"database":"PANTHER","id":"PTHR20856","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04565","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"RTVGEQLYNQFSIGLSRMARTVKERMNVRDSEVFTPVDLVNSKTIASVVNSFFGTNALSQFMDQQNPLSEITHKRRLSALGPGGLTRDRAGFEVRDVHYTHYGRL","length":105,"molWeight":11889,"crc64":"5534D35B1B068E85","md5":"EABD5E2C267E8BC64F32C5D49AB49D15"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0000401587"}}]}