ID   ATPF_PELPD              Reviewed;         202 AA.
AC   A1ALL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=atpF1 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=Ppro_0602;
GN   and
GN   Name=atpF2 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=Ppro_1503;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000482; ABK98233.1; -; Genomic_DNA.
DR   EMBL; CP000482; ABK99118.1; -; Genomic_DNA.
DR   RefSeq; WP_011734546.1; NC_008609.1.
DR   AlphaFoldDB; A1ALL3; -.
DR   SMR; A1ALL3; -.
DR   STRING; 338966.Ppro_0602; -.
DR   PRIDE; A1ALL3; -.
DR   EnsemblBacteria; ABK98233; ABK98233; Ppro_0602.
DR   EnsemblBacteria; ABK99118; ABK99118; Ppro_1503.
DR   KEGG; ppd:Ppro_0602; -.
DR   KEGG; ppd:Ppro_1503; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_3_2_7; -.
DR   OMA; NILNWAV; -.
DR   OrthoDB; 1530385at2; -.
DR   Proteomes; UP000006732; 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   Pfam; PF00430; 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..202
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_5000181802"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   202 AA;  22043 MW;  1A3EEE01D4FA1A8D CRC64;
     MGTPSDRTTT LSLCLAVCVV VIAVGTGWAS EAGEGAHQVD SAAQMKDFGW RVLNFAVLAA
     LLGWAIAKAQ VKKALNERQV KIERSLREAE QSRDAAEQKL REYSGKLEHA SREIEEMRGA
     MLRESEQEKQ RIIAEARAAA EKIAGQATLS AEHEVLKARS ALQAEAGRLA VQLAATKLAG
     AIGKEDHDLY VDDYLKKVEQ FK