ID   ATPF2_RHORU             Reviewed;         161 AA.
AC   P15015;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=ATP synthase subunit b';
DE   AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000303|PubMed:2902844};
DE   AltName: Full=ATPase subunit II;
DE   AltName: Full=F-type ATPase subunit b';
DE            Short=F-ATPase subunit b';
GN   Name=atpF2; Synonyms=atpF {ECO:0000303|PubMed:2902844}, atpG;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2902844; DOI=10.1042/bj2540109;
RA   Falk G., Walker J.E.;
RT   "DNA sequence of a gene cluster coding for subunits of the F0 membrane
RT   sector of ATP synthase in Rhodospirillum rubrum. Support for modular
RT   evolution of the F1 and F0 sectors.";
RL   Biochem. J. 254:109-122(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 (By similarity).
CC       {ECO:0000250}.
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       (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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DR   EMBL; M37308; AAA26457.1; -; Genomic_DNA.
DR   EMBL; X12757; CAA31248.1; -; Genomic_DNA.
DR   PIR; S01149; S01149.
DR   RefSeq; WP_011390992.1; NZ_NHSM01000219.1.
DR   AlphaFoldDB; P15015; -.
DR   SMR; P15015; -.
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   GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
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   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..161
FT                   /note="ATP synthase subunit b'"
FT                   /id="PRO_0000082427"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   161 AA;  17257 MW;  58CD6ADCCFEF8F0E CRC64;
     MPQFDPSSFP SQIVWLVIAL VAMYFVMSRL AIPRLAEVLE QRQRLINDDL KQAEALKAET
     EAAIAAYETA LAEARARAHD EIRAVTEAAA KAAEARNAEV AKALNTRIKD GEARIVQARD
     EALTHVREVA GAVASDIVGK LAGLRVDDAA LTAAVAAAIK E