{"metadata":{"accession":"PF02687","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003838","hierarchy":null,"name":{"name":"FtsX-like permease C-terminal","short":"FtsX"},"description":[{"text":"<p>This entry represents the C-terminal helices found in members of the ABC type 3 transporter family of permeases, including Cell division protein FtsX from Gram-negative and Gram-positive bacteria [[cite:PUB00096431]], Permease protein MacB [[cite:PUB00072503]], Lipoprotein-releasing system transmembrane protein LolC ([swissprot:P57382]) which  has been shown to transport lipids targeted to the outer membrane across the inner membrane [[cite:PUB00071889]]. This region contains three transmembrane helices.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00072505":{"PMID":10783239,"ISBN":null,"volume":"2","issue":"4","year":2000,"title":"A new ABC transporter mediating the detachment of lipid-modified proteins from membranes.","URL":null,"raw_pages":"212-8","medline_journal":"Nat Cell Biol","ISO_journal":"Nat. Cell Biol.","authors":["Yakushi T","Masuda K","Narita S","Matsuyama S","Tokuda H."],"DOI_URL":"http://dx.doi.org/10.1038/35008635"},"PUB00096431":{"PMID":19806386,"ISBN":null,"volume":"231","issue":"1","year":2009,"title":"Membrane porters of ATP-binding cassette transport systems are polyphyletic.","URL":null,"raw_pages":"1-10","medline_journal":"J Membr Biol","ISO_journal":"J Membr Biol","authors":["Wang B","Dukarevich M","Sun EI","Yen MR","Saier MH Jr."],"DOI_URL":null},"PUB00072503":{"PMID":19376877,"ISBN":null,"volume":"191","issue":"12","year":2009,"title":"ATP-binding site lesions in FtsE impair cell division.","URL":null,"raw_pages":"3772-84","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Arends SJ","Kustusch RJ","Weiss DS."],"DOI_URL":"http://dx.doi.org/10.1128/JB.00179-09"},"PUB00071889":{"PMID":18955484,"ISBN":null,"volume":"284","issue":"2","year":2009,"title":"MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA.","URL":null,"raw_pages":"1145-54","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lin HT","Bavro VN","Barrera NP","Frankish HM","Velamakanni S","van Veen HW","Robinson CV","Borges-Walmsley MI","Walmsley AR."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M806964200"}},"set_info":{"accession":"CL0404","name":"BPD_transp_1"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":129,"interactions":0,"matches":194321,"pathways":0,"proteins":143181,"proteomes":18550,"sets":1,"structural_models":{"alphafold":90109},"structures":72,"taxa":26730},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":63,"alignment:full":100550},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}