{"metadata":{"accession":"PF05947","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010272","hierarchy":null,"name":{"name":"Type VI secretion system, TssF","short":"T6SS_TssF"},"description":[{"text":"<p>This is a family of Gram-negative bacterial proteins that form part of the type VI pathogenicity secretion system (T6SS) , including TssF. TssF is homologues to phage tail proteins and is required for proper assembly of the Hcp tube (the T6SS inner tube) in bacteria [[cite:PUB00077772]]. 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]]. T6SSs contain 13 conserved components (TssA-TssM) which are thought to form the core apparatus and to enable effector proteins to be injected into target cells in a single cell-contact-dependent step.  TssF one of the core components of T6SSs machinery, has been shown to be recruited by TssK into the membrane-associated T6SS complex, contributing to the dynamic mechanism of the system [[cite:PUB00136430]]. Furthermore, it has been reported to interact with TssG proteins stabilizing each other while making contact with TssE, TssK and VgrG as well as with tube and sheath components. Bioinformatic analysis suggest that TssF and TssG share similarities with the J and I proteins of the bacteriophage P2 baseplate respectively. Further experimental studies show that functional TssF and TssK proteins assemble into static foci near the cell envelope. Moreover, biochemical and cytological approaches provide support to the role of TssE, TssF, TssG, TssK and VgrG as T6SS baseplate components and to a sequential recruitment hierarchy (membrane complex, baseplate, tail tube/sheath) during T6SS biogenesis [[cite:PUB00077772]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00067810":{"PMID":22184413,"ISBN":null,"volume":"80","issue":"3","year":2012,"title":"Hcp family proteins secreted via the type VI secretion system coordinately regulate Escherichia coli K1 interaction with human brain microvascular endothelial cells.","URL":null,"raw_pages":"1243-51","medline_journal":"Infect Immun","ISO_journal":"Infect. Immun.","authors":["Zhou Y","Tao J","Yu H","Ni J","Zeng L","Teng Q","Kim KS","Zhao GP","Guo X","Yao Y."],"DOI_URL":"http://dx.doi.org/10.1128/IAI.05994-11"},"PUB00077772":{"PMID":26460929,"ISBN":null,"volume":"11","issue":"10","year":2015,"title":"The Type VI Secretion TssEFGK-VgrG Phage-Like Baseplate Is Recruited to the TssJLM Membrane Complex via Multiple Contacts and Serves As Assembly Platform for Tail Tube/Sheath Polymerization.","URL":null,"raw_pages":"e1005545","medline_journal":"PLoS Genet","ISO_journal":"PLoS Genet.","authors":["Brunet YR","Zoued A","Boyer F","Douzi B","Cascales E."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pgen.1005545"},"PUB00136430":{"PMID":24779861,"ISBN":null,"volume":"461","issue":"2","year":2014,"title":"Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK-TssFG subcomplex.","URL":null,"raw_pages":"291-304","medline_journal":"Biochem J","ISO_journal":"Biochem J","authors":["English G","Byron O","Cianfanelli FR","Prescott AR","Coulthurst SJ."],"DOI_URL":null},"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"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":19,"interactions":0,"matches":5531,"pathways":0,"proteins":5516,"proteomes":3423,"sets":0,"structural_models":{"alphafold":3292},"structures":3,"taxa":4977},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":71,"alignment:full":1861},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}