ID   ATPF_BUCAP              Reviewed;         163 AA.
AC   O51876;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 130.
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=BUsg_004;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9216881; DOI=10.1007/s002849900217;
RA   Clark M.A., Baumann P.;
RT   "The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids):
RT   genetic analysis of the putative ATP operon.";
RL   Curr. Microbiol. 35:84-89(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01398};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-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; AF008210; AAC38114.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67576.1; -; Genomic_DNA.
DR   RefSeq; WP_011053542.1; NC_004061.1.
DR   AlphaFoldDB; O51876; -.
DR   SMR; O51876; -.
DR   STRING; 198804.BUsg_004; -.
DR   EnsemblBacteria; AAM67576; AAM67576; BUsg_004.
DR   KEGG; bas:BUsg_004; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_4_5_6; -.
DR   OMA; FAWKPIL; -.
DR   OrthoDB; 1999641at2; -.
DR   Proteomes; UP000000416; 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; 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 membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..163
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000082368"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT   CONFLICT        156..163
FT                   /note="LSKDKKLI -> FI (in Ref. 1; no nucleotide entry and
FT                   2; AAC38114)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   163 AA;  19075 MW;  3D4AE37A44255146 CRC64;
     MNLNATILGQ ALSFILFVWF CMKYIWPPII FAIETRQKNI EESLISLKKA EEELIIIQKK
     MNQIIQDSKE KASFIINEAN KKKSIILEDA KSIALEESKK IFLRNQLEID LKVMQVRKNL
     HKEIVDLSIL IAEKIIKDNI QKDQYKYSIK KLIVSLSKDK KLI