ID   ATPF_MOOTA              Reviewed;         168 AA.
AC   Q2RFX5; O05429;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Moth_2382;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND OPERON STRUCTURE.
RX   PubMed=9171425; DOI=10.1128/jb.179.11.3746-3755.1997;
RA   Das A., Ljungdahl L.G.;
RT   "Composition and primary structure of the F1F0 ATP synthase from the
RT   obligately anaerobic bacterium Clostridium thermoaceticum.";
RL   J. Bacteriol. 179:3746-3755(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; U64318; AAB51462.1; -; Genomic_DNA.
DR   EMBL; CP000232; ABC20664.1; -; Genomic_DNA.
DR   RefSeq; WP_011393859.1; NC_007644.1.
DR   RefSeq; YP_431207.1; NC_007644.1.
DR   AlphaFoldDB; Q2RFX5; -.
DR   SMR; Q2RFX5; -.
DR   STRING; 264732.Moth_2382; -.
DR   EnsemblBacteria; ABC20664; ABC20664; Moth_2382.
DR   GeneID; 61291105; -.
DR   KEGG; mta:Moth_2382; -.
DR   PATRIC; fig|264732.11.peg.2595; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_4_4_9; -.
DR   OMA; NILNWAV; -.
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   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..168
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000368592"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   168 AA;  18879 MW;  29D9CF0E81455238 CRC64;
     MQAIFQALNF NPWTFLFQTL NLLVVMGLLY VFLYKPLGKV LADREARIEG NLNDAAAARE
     KAENILAEYR QQLQGARQEA QAILDRATKM AEETRAEIIN RAREEAERTL AQARREIEGE
     KSKALAAIRS EAASLAILAA GKVLERSLTP DDQERLAREA IAEVERLQ