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ATPF_OLEA2
ID   ATPF_OLEA2              Reviewed;         192 AA.
AC   Q313V6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Dde_0989;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
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}.
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DR   EMBL; CP000112; ABB37790.1; -; Genomic_DNA.
DR   RefSeq; WP_011367031.1; NC_007519.1.
DR   AlphaFoldDB; Q313V6; -.
DR   SMR; Q313V6; -.
DR   STRING; 207559.Dde_0989; -.
DR   EnsemblBacteria; ABB37790; ABB37790; Dde_0989.
DR   KEGG; dde:Dde_0989; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_3_1_7; -.
DR   OMA; NILNWAV; -.
DR   OrthoDB; 1530385at2; -.
DR   Proteomes; UP000002710; Chromosome.
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; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR005864; ATP_synth_F0_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   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..192
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_5000102791"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   192 AA;  21339 MW;  EFD028EC0DF57020 CRC64;
     MKGLRKLLLV LGVMLLATGV ALAAGGEAAS GEHHYDWTNL GFRLANFAIF IAIIYYAAGK
     KLIAFFGGRR KGIEQELNDL ETRKTDAKKQ LGDVEKRIAD LENERKAIIA EYQAQGEALK
     AAIISKAETS ARQIVEQAKK SAENEVKYAK DAMREELADM IVDATEKLLK ERLDGKEQEK
     LIDKYLTKVV LN
 
 
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