ID   ATPB_CYTFI              Reviewed;         467 AA.
AC   P25075;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
OS   Cytobacillus firmus (Bacillus firmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=1399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RAB;
RX   PubMed=2181405; DOI=10.1093/nar/18.5.1296;
RA   Ivey D.M., Krulwich T.A.;
RT   "Sequence of the gene encoding the ATP synthase beta subunit from
RT   alkaliphilic Bacillus firmus RAB.";
RL   Nucleic Acids Res. 18:1296-1296(1990).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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_01347}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; M31107; AAA22253.1; -; Genomic_DNA.
DR   PIR; S12743; PWBSBF.
DR   AlphaFoldDB; P25075; -.
DR   SMR; P25075; -.
DR   PRIDE; P25075; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..467
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144418"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   CONFLICT        250
FT                   /note="D -> V (in Ref. 1; AAA22253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  50712 MW;  031D6C940602128F CRC64;
     MEYRSHISVM GPVVDVKFKS GQYPESINAL KSTSRVRQNA VDVTVTLEVA IALGDDSVRT
     VAMGSTDGLY VYRGTDTGAP ISVPVGEATL GRVFNVLGEA IDLGEPVAAD DKRDPIHREA
     PKFEELSTTT EILETGIKVV DLLAPYIIGG KIGLFGGAGV GKTVLIQELI NNIAQEHGVI
     SVFAGVGERT REGNDLYHEM TDSGVIKKSA MVFGQMNEPP GARMAVALSG LTMAEHFRDR
     DGQDVLLFVD NISFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STKVGSVTSI
     QAIYVPADDY TDPAPATTFA HLDATTNLER KLSEMGIYPA VDPLASTSRA LSPEIVGEEH
     YSVARQVQQT LQKYKELQDI IAILGMDELS EEDKLVVHRA RRIQFFLSQN FHVAEQFTGQ
     KGSYVPVKET IKGFKESLDG KYDDLPEDAF RLVGRIEEVI EKGKQTA