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It works in conjunction with other elongation-specific D,D-endopeptidases to make space for efficient incorporation of nascent peptidoglycan strands into the sacculus and thus enable cell wall expansion (PubMed:30940749). In vitro, is able to cleave the mDAP cross-links of soluble muropeptides and of intact peptidoglycan sacculi (PubMed:30940749). Shows a weak D,D-endopeptidase activity (PubMed:30940749)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q06241"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q06241"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30940749"}],"value":"Cell wall biogenesis; cell wall polysaccharide biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00648"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17218314"}],"value":"Exported by the Tat system (PubMed:17218314). The position of the signal peptide cleavage has not been experimentally proven (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30940749"}],"value":"The deletion mutant does not exhibit any discernible phenotype except a moderate increase in sensitivity to certain beta-lactam antibiotics such as ampicillin and cephalexin (PubMed:30940749). A double mepS-mepK deletion mutant bulges and lyses in low-osmolarity conditions (PubMed:30940749). A triple mepS-mepH-mepK deletion mutant grows very poorly with extensive lysis and cell death (PubMed:30940749)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M15 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Tat-type signal","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00648"}]},{"type":"Chain","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Peptidoglycan L,D-endopeptidase MepK","featureId":"PRO_0000168773"},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q06241"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q06241"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q06241"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Mutagenesis","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30940749"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30940749"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30940749"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"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":2,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. 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