{"metadata":{"accession":"PF05164","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007838","hierarchy":null,"name":{"name":"Cell division protein ZapA","short":"ZapA"},"description":[{"text":"<p>ZapA is a cell division protein which interacts with FtsZ.  FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle.  The interaction of FtsZ with ZapA drives its polymerisation and promotes FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring [[cite:PUB00021077]][[cite:PUB00021078]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"ZapA_family","extract":"<p>In molecular biology, the <b>ZapA protein family</b> is a group of related proteins that includes the cell division protein ZapA. The structure of ZapA has a core structure consisting of two layers alpha/beta, and has a long C-terminal helix that forms dimeric parallel and tetrameric antiparallel coiled coils. ZapA interacts with FtsZ, where FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. ZapA drives the polymerisation and filament bundling of FtsZ, thereby contributing to the spatio-temporal tuning of the Z-ring.</p>","thumbnail":null}],"literature":{"PUB00021078":{"PMID":12368265,"ISBN":null,"volume":"16","issue":"19","year":2002,"title":"A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.","URL":null,"raw_pages":"2544-56","medline_journal":"Genes Dev","ISO_journal":"Genes Dev.","authors":["Gueiros-Filho FJ","Losick R."],"DOI_URL":"http://dx.doi.org/10.1101/gad.1014102"},"PUB00021077":{"PMID":15288790,"ISBN":null,"volume":"341","issue":"3","year":2004,"title":"The crystal structure of ZapA and its modulation of FtsZ polymerisation.","URL":null,"raw_pages":"839-52","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Low HH","Moncrieffe MC","Lowe J."],"DOI_URL":"http://dx.doi.org/10.1016/j.jmb.2004.05.031"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":5,"interactions":0,"matches":12174,"pathways":0,"proteins":12174,"proteomes":11736,"sets":0,"structural_models":{"alphafold":8175},"structures":7,"taxa":16542},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":251,"alignment:full":5989},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"9isj","name":"Crystal structure of Klebsiella pneumoniae ZapA"}}}