ID   ATPB_STRR6              Reviewed;         468 AA.
AC   Q8DP44; Q8VSS0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
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}; OrderedLocusNames=spr1360;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=11580837; DOI=10.1046/j.1365-2958.2001.02597.x;
RA   Martin-Galiano A.J., Ferrandiz M.J., de la Campa A.G.;
RT   "The promoter of the operon encoding the F0F1 ATPase of Streptococcus
RT   pneumoniae is inducible by pH.";
RL   Mol. Microbiol. 41:1327-1338(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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, ECO:0000269|PubMed:11580837}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11580837};
CC       Peripheral membrane protein {ECO:0000305|PubMed:11580837}.
CC   -!- INDUCTION: Induced by a decrease in external pH from 7.5 to 5.7.
CC       {ECO:0000269|PubMed:11580837}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; AF368465; AAL66415.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAL00164.1; -; Genomic_DNA.
DR   PIR; F95175; F95175.
DR   PIR; G98041; G98041.
DR   RefSeq; NP_358953.1; NC_003098.1.
DR   RefSeq; WP_000094354.1; NC_003098.1.
DR   AlphaFoldDB; Q8DP44; -.
DR   SMR; Q8DP44; -.
DR   STRING; 171101.spr1360; -.
DR   EnsemblBacteria; AAL00164; AAL00164; spr1360.
DR   GeneID; 60232549; -.
DR   GeneID; 66806598; -.
DR   KEGG; spr:spr1360; -.
DR   PATRIC; fig|171101.6.peg.1474; -.
DR   eggNOG; COG0055; Bacteria.
DR   HOGENOM; CLU_022398_0_2_9; -.
DR   OMA; GFNMIMD; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..468
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000254390"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   CONFLICT        323
FT                   /note="D -> N (in Ref. 1; AAL66415)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  50904 MW;  AD58C147ADD63EF8 CRC64;
     MSSGKIAQVI GPVVDVLFAA GEKLPEINNA LVVYKNDERK TKIVLEVALE LGDGMVRTIA
     MESTDGLTRG MEVLDTGRPI SVPVGKETLG RVFNVLGDTI DLEAPFTEDA ERQPIHKKAP
     TFDELSTSSE ILETGIKVID LLAPYLKGGK VGLFGGAGVG KTVLIQELIH NIAQEHGGIS
     VFAGVGERTR EGNDLYWEMK ESGVIEKTAM VFGQMNEPPG ARMRVALTGL TIAEYFRDVE
     GQDVLLFIDN IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STKKGSVTSI
     QAIYVPADDY TDPAPATAFA HLDSTTNLER KLVQLGIYPA VDPLASSSRA LAPEIVGEEH
     YAVAAEVKRV LQRYHELQDI IAILGMDELS DEEKTLVARA RRIQFFLSQN FNVAEQFTGQ
     PGSYVPVAET VRGFKEILDG KYDHLPEDAF RGVGSIEDVI AKAEKMGF