ID A0A7Y8VBK2_9GAMM Unreviewed; 156 AA. AC A0A7Y8VBK2; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398}; DE AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398}; DE Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398, GN ECO:0000313|EMBL:NWO02180.1}; GN ORFNames=HLX52_04360 {ECO:0000313|EMBL:NWO02180.1}; OS Idiomarinaceae bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae. OX NCBI_TaxID=1898113 {ECO:0000313|EMBL:NWO02180.1, ECO:0000313|Proteomes:UP000526543}; RN [1] {ECO:0000313|EMBL:NWO02180.1, ECO:0000313|Proteomes:UP000526543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KG9 {ECO:0000313|EMBL:NWO02180.1}; RA Chun B.H., Jeon C.O.; RT "Metagenomic, metatranscriptomic, and metabolomic analyses revealed the key RT microbes and metabolic features during the fermentation of ganjang, Korean RT traditional soy sauce."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged CC and duplicated form of b found in plants and photosynthetic bacteria. CC {ECO:0000256|ARBA:ARBA00025614}. 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. CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398}; CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}. CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004167}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01398, CC ECO:0000256|RuleBase:RU003848}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NWO02180.1}. 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; JABXHH010000001; NWO02180.1; -; Genomic_DNA. DR SMR; A0A7Y8VBK2; -. DR Proteomes; UP000526543; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01398}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}. FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01398" FT COILED 40..82 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 156 AA; 17706 MW; DAFC2B50C7D8CFC4 CRC64; MNINATLIGQ TIAFIVFVWF CMKFVWPPII KAIEERQKKI ADGLNAGERA QKDLEKAQQE IAEQLKEAKQ QAAEIIEQSK KRGAKIVEEE TQRGHEEREK IVAAGHEEVA AERNRVREEL RKQVAVLAVS GAQKIIEREI DKDAHSDIVE KLVAEL //