{"metadata":{"accession":"PF07126","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR048372","hierarchy":null,"name":{"name":"Cell-division protein ZapC, C-terminal","short":"ZapC_C"},"description":[{"text":"<p>ZapC is one of four FtsZ-binding components of the Z ring in bacteria. Formation of the Z ring on the cytoplasmic surface of the membrane is the starting process for assembly of the cell-division apparatus. It binds directly to the Z ring, and although it is not essential for absolute cell division it contributes to it by enhancing the interactions between the FtsZ protofilaments (or polymers) which aggregate to form the ring conformation in the Z ring [[cite:PUB00060666]]. This is the C-terminal domain which contains a pocket with a hydrophobic centre surrounded by conserved basic residues, critical for FtsZ binding [[cite:PUB00101038],[cite:PUB00101039]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00101039":{"PMID":26619764,"ISBN":null,"volume":"589","issue":"24 Pt B","year":2015,"title":"Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.","URL":null,"raw_pages":"3822-8","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett","authors":["Ortiz C","Kureisaite-Ciziene D","Schmitz F","McLaughlin SH","Vicente M","Lowe J."],"DOI_URL":null},"PUB00101038":{"PMID":26655719,"ISBN":null,"volume":"291","issue":"5","year":2016,"title":"Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.","URL":null,"raw_pages":"2485-98","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Schumacher MA","Zeng W","Huang KH","Tchorzewski L","Janakiraman A."],"DOI_URL":null},"PUB00060666":{"PMID":21216997,"ISBN":null,"volume":"193","issue":"6","year":2011,"title":"Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers.","URL":null,"raw_pages":"1393-404","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Hale CA","Shiomi D","Liu B","Bernhardt TG","Margolin W","Niki H","de Boer PA."],"DOI_URL":"http://dx.doi.org/10.1128/JB.01245-10"}},"set_info":{"accession":"CL0010","name":"SH3"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":2,"interactions":0,"matches":1065,"pathways":0,"proteins":1065,"proteomes":1061,"sets":1,"structural_models":{"alphafold":670},"structures":2,"taxa":1410},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":24,"alignment:full":309},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}