{"metadata":{"accession":"PF01944","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002798","hierarchy":null,"name":{"name":"Stage II sporulation protein M","short":"SpoIIM"},"description":[{"text":"<p>SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalised through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, [pfam:PF05036], SpoIIM, SpoIIP, [pfam:PF07454], and finally SpoIID, [pfam:PF08486]. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum [[cite:PUB00109154]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00109154":{"PMID":17376078,"ISBN":null,"volume":"64","issue":"1","year":2007,"title":"Engulfment during sporulation in Bacillus subtilis is governed by a multi-protein complex containing tandemly acting autolysins.","URL":null,"raw_pages":"139-52","medline_journal":"Mol Microbiol","ISO_journal":"Mol Microbiol","authors":["Chastanet A","Losick R."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":14,"interactions":0,"matches":8865,"pathways":0,"proteins":8861,"proteomes":7738,"sets":0,"structural_models":{"alphafold":5639},"structures":0,"taxa":10914},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":263,"alignment:full":4483},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}