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Specifically hydrolyzes the natural, peptidoglycan-derived disaccharide MurNAc-GlcNAc and the artificial substrate para-nitrophenyl beta-N-acetylmuramic acid (pNP-MurNAc) (PubMed:33684445). Requires a MurNAc entity at the non-reducing end, and cannot cleave GlcNAc-MurNAc (PubMed:33684445). Probably plays a role in cell wall turnover and recycling (PubMed:33684445)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal, non-reducing N-acetylmuramic residues.","ecNumber":"3.2.1.92","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":88.64,"unit":"umol/min/mg","enzyme":"enzyme with MurNAc-GlcNAc as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}]},{"velocity":1.45,"unit":"umol/min/mg","enzyme":"enzyme with pNP-MurNAc as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}]}],"michaelisConstants":[{"constant":3.59,"unit":"mM","substrate":"MurNAc-GlcNAc","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}]},{"constant":0.125,"unit":"mM","substrate":"pNP-MurNAc","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"kcat is 66.25 sec(-1) with MurNAc-GlcNAc as substrate (PubMed:33684445). kcat is 1.08 sec(-1) with pNP-MurNAc as substrate (PubMed:33684445)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"Optimum pH is 6.0-8.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"Optimum temperature is 37 degrees Celsius. Stable from 4 to 37 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"Homodimer in solution"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33684445"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"Contains an N-terminal catalytic domain and a C-terminal auxiliary domain (PubMed:33684445). A putative active site is located in a cleft within the interface of two subdomains (PubMed:33684445)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684445"}],"value":"Deletion mutant accumulates specific cell wall fragments and shows growth defects under starvation conditions"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33684445"}],"value":"Belongs to the glycoside hydrolase 171 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"Peptidoglycan beta-N-acetylmuramidase NamZ","featureId":"PRO_0000013689"}],"keywords":[{"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"8011666","citationType":"journal article","authors":["Quirk P.G.","Guffanti A.A.","Clejan S.","Cheng J.","Krulwich T.A."],"citationCrossReferences":[{"database":"PubMed","id":"8011666"},{"database":"DOI","id":"10.1016/0005-2728(94)90131-7"}],"title":"Isolation of Tn917 insertional mutants of Bacillus subtilis that are resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.","publicationDate":"1994","journal":"Biochim. 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