{"metadata":{"accession":"PF07075","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR048502","hierarchy":null,"name":{"name":"Exo-beta-N-acetylmuramidase NamZ, N-terminal","short":"NamZ_N"},"description":[{"text":"<p>NamZ is an exo-beta-N-acetylmuramidase which catalyzes an exo-lytic cleavage of beta-1,4-acetylmuramic acid from from the non-reducing ends of peptidoglycan chains [[cite:PUB00100156]] and it is a founding member of a new family of glycosidases (GH171). NamZ consists of a N-terminal catalytic domain with a Rossmann-like fold (represented in this entry) and a C-terminal auxiliary alpha/beta domain [[cite:PUB00100156]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100156":{"PMID":33684445,"ISBN":null,"volume":"296","issue":null,"year":2021,"title":"The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases.","URL":null,"raw_pages":"100519","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Muller M","Calvert M","Hottmann I","Kluj RM","Teufel T","Balbuchta K","Engelbrecht A","Selim KA","Xu Q","Borisova M","Titz A","Mayer C."],"DOI_URL":null}},"set_info":{"accession":"CL0063","name":"NADP_Rossmann"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":34,"interactions":0,"matches":6295,"pathways":0,"proteins":6284,"proteomes":5412,"sets":1,"structural_models":{"alphafold":3928},"structures":2,"taxa":7889},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":191,"alignment:full":3225},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4jja","name":"Crystal structure of a DUF1343 family protein (BF0379) from Bacteroides fragilis NCTC 9343 at 1.30 A resolution"}}}