{"metadata":{"accession":"PF13036","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR014094","hierarchy":null,"name":{"name":"Peptidoglycan-synthase activator LpoB","short":"LpoB"},"description":[{"text":"<p>This is a family of Gram-negative bacterial outer membrane lipoproteins. LpoB is required for the function of the major peptidoglycan synthase enzyme PBP1B. It interacts with PBP1B protein via the UvrB-like non-catalytic domain on that protein. LpoB has a 54-aa-long flexible N-terminal stretch followed by a globular domain with similarity to the N-terminal domain of the prevalent periplasmic protein TolB. The long, flexible N-terminal region of LpoB enables it to span the periplasm and reach its docking site in PBP1B.  Peptidoglycan is the essential polymer within the sacculus that surrounds the cytoplasmic membrane of bacteria [[cite:PUB00110446]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00110446":{"PMID":24821816,"ISBN":null,"volume":"111","issue":"22","year":2014,"title":"Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B.","URL":null,"raw_pages":"8197-202","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Egan AJ","Jean NL","Koumoutsi A","Bougault CM","Biboy J","Sassine J","Solovyova AS","Breukink E","Typas A","Vollmer W","Simorre JP."],"DOI_URL":null}},"set_info":{"accession":"CL0342","name":"TolB_N"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":14,"interactions":0,"matches":2478,"pathways":0,"proteins":2477,"proteomes":2269,"sets":1,"structural_models":{"alphafold":1619},"structures":6,"taxa":3652},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":31,"alignment:full":1040},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4q6v","name":"LpoB C-terminal domain from Salmonella enterica (Sel-Met)"}}}