{"metadata":{"accession":"PF05591","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR008312","hierarchy":null,"name":{"name":"Type VI secretion system, VipA, VC_A0107 or Hcp2","short":"T6SS_VipA"},"description":[{"text":"<p>T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex [[cite:PUB00090998]]. VipA is a family of Gram-negative bacterial proteins that form part of the type VI pathogenic secretion system. Members have been variously defined as VC_A0107 family, Hcp2, TssB and VipA, for ClpV-interacting proteins. VipB and VipA proteins interact very closely to form the shaft of the pathogenic penetrating needle system [[cite:PUB00075705],[cite:PUB00075433],[cite:PUB00075706]]. VipA and VipB (TssB and TssC) proteins were shown to form a cog-wheel like tubular structure in V. cholerae that was noticed to resemble T4 phage gp18 polysheath. Two beta-strands of VipA and four beta-strands of VipB intertwine forming the middle layer of the sheath. The sheath assembles around an inner Hcp tube and is attached to a structure called a baseplate that spans the bacterial membranes. Importantly, VipA/VipB sheath was shown to form a long contractile organelle in V. cholerae and in E. coli, suggesting that sheath contraction powers the secretion [[cite:PUB00091000]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00075433":{"PMID":18289922,"ISBN":null,"volume":"11","issue":"1","year":2008,"title":"Type VI secretion: a beginner's guide.","URL":null,"raw_pages":"3-8","medline_journal":"Curr Opin Microbiol","ISO_journal":"Curr. Opin. Microbiol.","authors":["Bingle LE","Bailey CM","Pallen MJ."],"DOI_URL":"http://dx.doi.org/10.1016/j.mib.2008.01.006"},"PUB00075706":{"PMID":23289512,"ISBN":null,"volume":"87","issue":"5","year":2013,"title":"ClpV recycles VipA/VipB tubules and prevents non-productive tubule formation to ensure efficient type VI protein secretion.","URL":null,"raw_pages":"1013-28","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Kapitein N","Bonemann G","Pietrosiuk A","Seyffer F","Hausser I","Locker JK","Mogk A."],"DOI_URL":"http://dx.doi.org/10.1111/mmi.12147"},"PUB00090998":{"PMID":26768901,"ISBN":null,"volume":"17","issue":null,"year":2016,"title":"Type VI secretion systems of human gut Bacteroidales segregate into three genetic architectures, two of which are contained on mobile genetic elements.","URL":null,"raw_pages":"58","medline_journal":"BMC Genomics","ISO_journal":"BMC Genomics","authors":["Coyne MJ","Roelofs KG","Comstock LE."],"DOI_URL":"https://doi.org/10.1186/s12864-016-2377-z"},"PUB00091000":{"PMID":25723169,"ISBN":null,"volume":"160","issue":"5","year":2015,"title":"Structure of the type VI secretion system contractile sheath.","URL":null,"raw_pages":"952-962","medline_journal":"Cell","ISO_journal":"Cell","authors":["Kudryashev M","Wang RY","Brackmann M","Scherer S","Maier T","Baker D","DiMaio F","Stahlberg H","Egelman EH","Basler M."],"DOI_URL":"https://doi.org/10.1016/j.cell.2015.01.037"},"PUB00075705":{"PMID":1913969,"ISBN":null,"volume":"14","issue":"3","year":1991,"title":"[Study on BCG vaccination and incidence of children's tuberculous meningitis in Liaoning province]","URL":null,"raw_pages":"173-5, 192","medline_journal":"Zhonghua Jie He He Hu Xi Za Zhi","ISO_journal":"Zhonghua Jie He He Hu Xi Za Zhi","authors":["Wu QR."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":12,"interactions":0,"matches":5021,"pathways":0,"proteins":4990,"proteomes":3299,"sets":0,"structural_models":{"alphafold":3141},"structures":11,"taxa":4768},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":78,"alignment:full":1787},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4uqz","name":"Coevolution of the ATPase ClpV, the TssB-TssC Sheath and the Accessory HsiE Protein Distinguishes Two Type VI Secretion Classes"}}}