{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P76008","secondaryAccessions":["O87499"],"uniProtkbId":"LDCA_ECOLI","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-02-01","entryVersion":167,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Murein tetrapeptide carboxypeptidase"},"ecNumbers":[{"value":"3.4.17.13"}]},"alternativeNames":[{"fullName":{"value":"LD-carboxypeptidase A"}},{"fullName":{"value":"Muramoyltetrapeptide carboxypeptidase"}}]},"genes":[{"geneName":{"value":"ldcA"},"synonyms":[{"value":"ycgQ"}],"orderedLocusNames":[{"value":"b1192"},{"value":"JW1181"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18535144"}],"value":"Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-meso-2,6-diaminoheptanedioyl-D-alanine + H2O = N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-meso-2,6-diaminoheptanedioate + D-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48688"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:233808"},{"database":"ChEBI","id":"CHEBI:233809"}],"ecNumber":"3.4.17.13","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"}],"value":"Inhibited by beta-lactams containing a D-amino acid side chain"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"}],"value":"Cell wall biogenesis; peptidoglycan recycling"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428950"}],"value":"Bacteriolysis during the stationary growth phase. Cells lacking this gene also accumulate UDP-MurNAc-tetrapeptide, an unusual compound that normally is not present at significant levels in E.coli cells"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase S66 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Murein tetrapeptide carboxypeptidase","featureId":"PRO_0000172837"},{"type":"Active site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Turn","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Turn","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Turn","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Helix","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]},{"type":"Beta strand","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5Z01"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0121","category":"Molecular function","name":"Carboxypeptidase"},{"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"10428950","citationType":"journal article","authors":["Templin M.F.","Ursinus A.","Hoeltje J.-V."],"citationCrossReferences":[{"database":"PubMed","id":"10428950"},{"database":"DOI","id":"10.1093/emboj/18.15.4108"}],"title":"A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli.","publicationDate":"1999","journal":"EMBO J.","firstPage":"4108","lastPage":"4117","volume":"18"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION IN MUREIN RECYCLING","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","ACTIVITY REGULATION","PATHWAY","DISRUPTION PHENOTYPE","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8905232","citationType":"journal article","authors":["Oshima T.","Aiba H.","Baba T.","Fujita K.","Hayashi K.","Honjo A.","Ikemoto K.","Inada T.","Itoh T.","Kajihara M.","Kanai K.","Kashimoto K.","Kimura S.","Kitagawa M.","Makino K.","Masuda S.","Miki T.","Mizobuchi K.","Mori H.","Motomura K.","Nakamura Y.","Nashimoto H.","Nishio Y.","Saito N.","Sampei G.","Seki Y.","Tagami H.","Takemoto K.","Wada C.","Yamamoto Y.","Yano M.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"8905232"},{"database":"DOI","id":"10.1093/dnares/3.3.137"}],"title":"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.","publicationDate":"1996","journal":"DNA Res.","firstPage":"137","lastPage":"155","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"18535144","citationType":"journal article","authors":["Park J.T.","Uehara T."],"citationCrossReferences":[{"database":"PubMed","id":"18535144"},{"database":"DOI","id":"10.1128/mmbr.00027-07"}],"title":"How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan).","publicationDate":"2008","journal":"Microbiol. Mol. Biol. Rev.","firstPage":"211","lastPage":"227","volume":"72"},"referencePositions":["FUNCTION IN PEPTIDOGLYCAN RECYCLING","REVIEW"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC74276.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA36050.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"E64865","properties":[{"key":"EntryName","value":"E64865"}]},{"database":"RefSeq","id":"NP_415710.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000051560.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"PDB","id":"5Z01","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A=1-304"}]},{"database":"PDB","id":"5Z03","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A/B=1-304"}]},{"database":"PDBsum","id":"5Z01","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5Z03","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P76008","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P76008","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4259643","properties":[{"key":"Interactions","value":"326"}]},{"database":"BioGRID","id":"850123","properties":[{"key":"Interactions","value":"1"}]},{"database":"DIP","id":"DIP-10085N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P76008","properties":[{"key":"Number of interactors","value":"332"}]},{"database":"IntAct","id":"P76008","properties":[{"key":"Interactions","value":"4"}]},{"database":"STRING","id":"511145.b1192","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"S66.002","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"P76008","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b1192","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC74276","properties":[{"key":"ProteinId","value":"AAC74276"},{"key":"GeneId","value":"b1192"}]},{"database":"GeneID","id":"945756","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW1181","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b1192","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_07015","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.1094","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB3657","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1619","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_034346_0_1_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P76008","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"MLTQWRL","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9807329at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P76008","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:G6621-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:G6621-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00544","properties":[{"key":"RectionId","value":"-"}]},{"database":"PRO","id":"PR:P76008","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10428950"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"18304323"}]},{"database":"GO","id":"GO:0004180","properties":[{"key":"GoTerm","value":"F:carboxypeptidase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"1729236"}]},{"database":"GO","id":"GO:0106415","properties":[{"key":"GoTerm","value":"F:muramoyltetrapeptide carboxypeptidase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10428950"}]},{"database":"GO","id":"GO:0061787","properties":[{"key":"GoTerm","value":"F:peptidoglycan cross-bridge peptide endopeptidase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"34933456"}]},{"database":"GO","id":"GO:0042803","properties":[{"key":"GoTerm","value":"F:protein homodimerization activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"29601819"}]},{"database":"GO","id":"GO:0009254","properties":[{"key":"GoTerm","value":"P:peptidoglycan turnover"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10428950"}]},{"database":"CDD","id":"cd07025","properties":[{"key":"EntryName","value":"Peptidase_S66"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10740:FF:000001","properties":[{"key":"EntryName","value":"Murein tetrapeptide carboxypeptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.60:FF:000001","properties":[{"key":"EntryName","value":"Murein tetrapeptide carboxypeptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10740","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.60","properties":[{"key":"EntryName","value":"LD-carboxypeptidase A C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027461","properties":[{"key":"EntryName","value":"Carboxypeptidase_A_C_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR027478","properties":[{"key":"EntryName","value":"LdcA_N"}]},{"database":"InterPro","id":"IPR040449","properties":[{"key":"EntryName","value":"Peptidase_S66_N"}]},{"database":"InterPro","id":"IPR040921","properties":[{"key":"EntryName","value":"Peptidase_S66C"}]},{"database":"InterPro","id":"IPR003507","properties":[{"key":"EntryName","value":"S66_fam"}]},{"database":"NCBIfam","id":"NF008424","properties":[{"key":"EntryName","value":"PRK11253.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30237","properties":[{"key":"EntryName","value":"MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30237:SF2","properties":[{"key":"EntryName","value":"MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02016","properties":[{"key":"EntryName","value":"Peptidase_S66"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17676","properties":[{"key":"EntryName","value":"Peptidase_S66C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF028757","properties":[{"key":"EntryName","value":"LD-carboxypeptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF141986","properties":[{"key":"EntryName","value":"LD-carboxypeptidase A C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM","length":304,"molWeight":33567,"crc64":"BD801CA75E2AC25F","md5":"A9A7D65AC76C76ECA701A94C40BF1A04"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":3,"Beta strand":16,"Helix":15,"Turn":3},"uniParcId":"UPI000012E2D1"}}