{"metadata":{"accession":"PF06005","entry_id":null,"type":"coiled_coil","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR009252","hierarchy":null,"name":{"name":"ZapB family","short":"ZapB"},"description":[{"text":"<p>The ZapB family consists of non-essential, abundant cell division proteins that play a crucial role in the formation of the Z-ring during bacterial cell division. These proteins are recruited early to the divisome through direct interaction with FtsZ, a key protein in the assembly of the Z-ring. By stimulating Z-ring assembly, ZapB proteins promote cell division earlier in the cell cycle. Their recruitment to the Z-ring is dependent on the presence of functional FtsA or ZipA proteins. Structurally, ZapB proteins form homodimers, with the ends of the coiled-coil dimers binding to each other to form polymers. This polymerization is essential for their function in cell division [[cite:PUB00078060]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00078060":{"PMID":18394147,"ISBN":null,"volume":"68","issue":"3","year":2008,"title":"Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division.","URL":null,"raw_pages":"720-35","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Ebersbach G","Galli E","Moller-Jensen J","Lowe J","Gerdes K."],"DOI_URL":"http://dx.doi.org/10.1111/j.1365-2958.2008.06190.x"}},"set_info":{"accession":"CL0225","name":"FtsL"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":2,"interactions":0,"matches":1534,"pathways":0,"proteins":1534,"proteomes":1468,"sets":1,"structural_models":{"alphafold":1054},"structures":1,"taxa":2333},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":26,"alignment:full":533},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}