ID ATPF_LEPBA Reviewed; 174 AA. AC B0SDA1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 22-SEP-2009, entry version 13. DE RecName: Full=ATP synthase subunit b; DE AltName: Full=ATP synthase F(0) sector subunit b; DE AltName: Full=F-type ATPase subunit b; DE Short=F-ATPase subunit b; DE AltName: Full=ATPase subunit I; GN Name=atpF; OrderedLocusNames=LBF_0774; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., RA McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., RA Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides RT insights into the evolution of Leptospira and the pathogenesis of RT leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation (By similarity). CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0) (By similarity). CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains (By similarity). CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000777; ABZ93306.1; -; Genomic_DNA. DR RefSeq; YP_001961884.1; -. DR GeneID; 6387860; -. DR GenomeReviews; CP000777_GR; LBF_0774. DR KEGG; lbf:LBF_0774; -. DR OMA; B0SDA1; ESIRMES. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, c...; IEA:InterPro. DR GO; GO:0046933; F:hydrogen ion transporting ATP synthase acti...; IEA:HAMAP. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR HAMAP; MF_01398; -; 1. DR InterPro; IPR002146; ATPase_F0-cplx_b/b'su_bac. DR InterPro; IPR005864; ATPase_F0-cplx_bsu_bac. DR Pfam; PF00430; ATP-synt_B; 1. DR TIGRFAMs; TIGR01144; ATP_synt_b; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Transmembrane; Transport. FT CHAIN 1 174 ATP synthase subunit b. FT /FTId=PRO_0000368558. FT TRANSMEM 15 33 Potential. SQ SEQUENCE 174 AA; 19602 MW; 077D71E4BE9C27B9 CRC64; MVLLAASGFN LLKVNPGLVI WTLVTFSVVV FVLKKFAWDK ILHALEERAS GIQGDINKAE SLRVEAEKSL KEYKDQLFKA TEEAHRIVDE AKKDAVALRT KLTEEAHNEV KGIKDSAVRE IELAKGRALS EIQNQIVEMS VLIASEILEK QLKKEDYASF VEKEIAKLDK LKIK //