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 03-AUG-2022, entry version 77. DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=LBF_0774; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / Ames; 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., McGrath A., RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides insights RT into the evolution of Leptospira and the pathogenesis of leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence CC of a proton or sodium gradient. F-type ATPases consist of two CC structural domains, F(1) containing the extramembraneous catalytic core CC and F(0) containing the membrane proton channel, linked together by a CC central stalk and a peripheral stalk. During catalysis, ATP synthesis CC in the catalytic domain of F(1) is coupled via a rotary mechanism of CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core CC - and F(0) - the membrane proton channel. F(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an CC alternating ring which encloses part of the gamma chain. F(1) is CC attached to F(0) by a central stalk formed by the gamma and epsilon CC chains, while a peripheral stalk is formed by the delta and b chains. CC {ECO:0000255|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP- CC Rule:MF_01398}. 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; WP_012387816.1; NC_010842.1. DR AlphaFoldDB; B0SDA1; -. DR SMR; B0SDA1; -. DR KEGG; lbf:LBF_0774; -. DR HOGENOM; CLU_079215_4_1_12; -. DR OMA; FAWKPIL; -. DR BioCyc; LBIF355278:LBF_RS03950-MON; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR HAMAP; MF_01398; ATP_synth_b_bprime; 1. DR InterPro; IPR028987; ATP_synth_B-like_membr_sf. DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt. DR InterPro; IPR005864; ATP_synth_F0_bsu_bac. DR Pfam; PF00430; ATP-synt_B; 1. DR SUPFAM; SSF81573; SSF81573; 1. DR TIGRFAMs; TIGR01144; ATP_synt_b; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Hydrogen ion transport; Ion transport; Membrane; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..174 FT /note="ATP synthase subunit b" FT /id="PRO_0000368558" FT TRANSMEM 15..33 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398" 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 //