ID   ATP6_RHOCA              Reviewed;         237 AA.
AC   O05330;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=9818357; DOI=10.1007/s002030050657;
RA   Borghese R., Turina P., Lambertini L., Melandri B.A.;
RT   "The atpIBEXF operon coding for the Fo sector of the ATP synthase from the
RT   purple nonsulfur photosynthetic bacterium Rhodobacter capsulatus.";
RL   Arch. Microbiol. 170:385-388(1998).
RN   [2]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=GA;
RA   Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.;
RT   "Purification of the H+-ATPase from Rhodobacter capsulatus, identification
RT   of the F1F0 components and reconstitution of the active enzyme.";
RL   Biochim. Biophys. Acta 934:227-234(1988).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(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_01393}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC       {ECO:0000269|Ref.2}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01393, ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
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DR   EMBL; Y12313; CAA72981.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05330; -.
DR   SMR; O05330; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore 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   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..237
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000239035"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   237 AA;  26096 MW;  CB623F47295F4862 CRC64;
     MFDGEAIRWF EFFVPTNSTL WMAIGVLMIA LLMVVGTLRR AIVPGRIQSL AELTYGFIHK
     MVEDVAGKDG LVYFPYIFTL FLFILFSNFL GLIPMAFTPT SHIAVTGVMA MGVFIGVTAL
     GFMKHGSHFL NLFWVSAAPL PLRPILAVIE VISYFVRPVS HSIRLAGNMM AGHAVMEVFA
     AFAPLILFSF VGVIVTPLSV LAIVAMYALE ILVAFVQAYV FTILTCVYLK DALHPGH