{"metadata":{"accession":"PF11983","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021873","hierarchy":null,"name":{"name":"Cell division protein FtsA, C-terminal","short":"FtsA_C"},"description":[{"text":"<p>This family is the C-terminal region of essential streptococcal FtsA proteins and their homologues. It acts as an intra-molecular switch, triggered by ATP, to promote polymerisation of the whole protein and to attach it to the membrane. FtsA is essential for the formation of the septum that divides fully-grown cells into two daughter cells at cell-division. FtsA anchors the constricting FtsZ ring to the membrane [[cite:PUB00078723]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"FtsA","extract":"<p><b>FtsA</b> is a bacterial protein that is related to actin by overall structural similarity and in its ATP binding pocket. It is involved in bacterial cell division, where it serves to tether the cytokinetic ring formed by FtsZ to the cytoplasmic membrane prior to division.</p>","thumbnail":null}],"literature":{"PUB00078723":{"PMID":25425238,"ISBN":null,"volume":"5","issue":"6","year":2014,"title":"Role of the FtsA C terminus as a switch for polymerization and membrane association.","URL":null,"raw_pages":"e02221","medline_journal":"MBio","ISO_journal":"MBio","authors":["Krupka M","Cabre EJ","Jimenez M","Rivas G","Rico AI","Vicente M."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":3,"interactions":0,"matches":347,"pathways":0,"proteins":347,"proteomes":344,"sets":0,"structural_models":{"alphafold":223},"structures":0,"taxa":469},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":12,"alignment:full":123},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}