{"metadata":{"accession":"PF05951","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010275","hierarchy":null,"name":{"name":"Peptidoglycan L,D-endopeptidase MepK","short":"Peptidase_M15_2"},"description":[{"text":"<p>This family represents Peptidoglycan L,D-endopeptidase MepK from Escherichia coli and similar bacterial proteins. MepK cleaves meso-diaminopimelic acid cross-links in peptidoglycan. It acts in conjunction with other elongation-specific D, D-endopeptidases to create space for the efficient incorporation of nascent peptidoglycan strands into the sacculus, thereby enabling cell wall expansion [[cite:PUB00160786]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00160786":{"PMID":30940749,"ISBN":null,"volume":"116","issue":"16","year":2019,"title":"Peptidoglycan hydrolase of an unusual cross-link cleavage specificity contributes to bacterial cell wall synthesis.","URL":null,"raw_pages":"7825-7830","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Chodisetti PK","Reddy M."],"DOI_URL":"https://doi.org/10.1073/pnas.1816893116"}},"set_info":{"accession":"CL0170","name":"Peptidase_MD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":7,"interactions":0,"matches":3871,"pathways":0,"proteins":3871,"proteomes":3319,"sets":1,"structural_models":{"alphafold":2536},"structures":0,"taxa":4791},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":7,"alignment:full":1873},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}