ID   ATPF_RHOCA              Reviewed;         185 AA.
AC   O05333;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 89.
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};
DE   Flags: Precursor;
GN   Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398};
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   PROTEIN SEQUENCE OF 20-41, 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: 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 four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is 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, b and b'
CC       chains. {ECO:0000255|HAMAP-Rule:MF_01398, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC       {ECO:0000269|Ref.2}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01398, ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
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DR   EMBL; Y12313; CAA72984.1; -; Genomic_DNA.
DR   RefSeq; WP_013066488.1; NZ_VIBE01000017.1.
DR   AlphaFoldDB; O05333; -.
DR   SMR; O05333; -.
DR   GeneID; 31489688; -.
DR   OMA; KVPGMMA; -.
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   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..19
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000239036"
FT   CHAIN           20..185
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000239037"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT   CONFLICT        20
FT                   /note="E -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="V -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   185 AA;  19802 MW;  9856ADF489B0CB59 CRC64;
     MKKLTFLLVA LAANPAFASE GPFVSLRNAH FVILVAFLIF VGVLIKFKVP SMLLGMLDKR
     AEGIKADLDE AKALRDEAQK ILASYERKAR EVQGQADEIV AAAKRDAQLA AEQAKADLKE
     AIARRLKGAE DRIASAEAAA LKDVKDRAVQ VAVAAAAEVL ANQMSASDKS GMIDAAITEV
     ETRLN