ID   ATPB_BACSU              Reviewed;         473 AA.
AC   P37809;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 156.
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};
DE   AltName: Full=Vegetative protein 31;
DE            Short=VEG31;
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=BSU36810;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7961438; DOI=10.1128/jb.176.22.6802-6811.1994;
RA   Santana M., Ionescu M.S., Vertes A., Longin R., Kunst F., Danchin A.,
RA   Glaser P.;
RT   "Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and
RT   characterization of atp mutants.";
RL   J. Bacteriol. 176:6802-6811(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-11.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPOIIIJ AND YQJG.
RC   STRAIN=168;
RX   PubMed=19717609; DOI=10.1128/jb.00853-09;
RA   Saller M.J., Fusetti F., Driessen A.J.;
RT   "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT   biogenesis.";
RL   J. Bacteriol. 191:6749-6757(2009).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=20713508; DOI=10.1101/gad.1945010;
RA   Lopez D., Kolter R.;
RT   "Functional microdomains in bacterial membranes.";
RL   Genes Dev. 24:1893-1902(2010).
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       (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA
CC       is found in the same complex. {ECO:0000255|HAMAP-Rule:MF_01347,
CC       ECO:0000269|PubMed:19717609, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347,
CC       ECO:0000269|PubMed:20713508}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01347}. Membrane raft
CC       {ECO:0000269|PubMed:20713508}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Present in detergent-resistant membrane (DRM)
CC       fractions that may be equivalent to eukaryotic membrane rafts; these
CC       rafts include proteins involved in signaling, molecule trafficking and
CC       protein secretion. {ECO:0000269|PubMed:20713508}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; Z28592; CAA82260.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15698.1; -; Genomic_DNA.
DR   PIR; I40368; I40368.
DR   RefSeq; NP_391562.1; NC_000964.3.
DR   RefSeq; WP_003227686.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P37809; -.
DR   SMR; P37809; -.
DR   IntAct; P37809; 3.
DR   MINT; P37809; -.
DR   STRING; 224308.BSU36810; -.
DR   jPOST; P37809; -.
DR   PaxDb; P37809; -.
DR   PRIDE; P37809; -.
DR   EnsemblBacteria; CAB15698; CAB15698; BSU_36810.
DR   GeneID; 936992; -.
DR   KEGG; bsu:BSU36810; -.
DR   PATRIC; fig|224308.179.peg.3987; -.
DR   eggNOG; COG0055; Bacteria.
DR   InParanoid; P37809; -.
DR   OMA; GFNMIMD; -.
DR   PhylomeDB; P37809; -.
DR   BioCyc; BSUB:BSU36810-MON; -.
DR   SABIO-RK; P37809; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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);
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..473
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000144425"
FT   BINDING         158..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   473 AA;  51420 MW;  EF1EFB6B900A099A CRC64;
     MKKGRVSQVL GPVVDVRFED GHLPEIYNAI KISQPAASEN EVGIDLTLEV ALHLGDDTVR
     TIAMASTDGV QRGMEAVDTG APISVPVGDV TLGRVFNVLG ENIDLNEPVP ADAKKDPIHR
     QAPSFDQLST EVEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LINNIAQEHG
     GISVFAGVGE RTREGNDLFY EMSDSGVINK TAMVFGQMNE PPGARMRVAL TGLTMAEHFR
     DVQGQDVLFF IDNIFRFTQA GSEVSALLGR MPSAVGYQPT LATEMGQLQE RITSTNVGSV
     TSIQAIYVPA DDYTDPAPAT TFAHLDATTN LERKLTEMGI YPAVDPLAST SRALAPEIVG
     EEHYAVAREV QSTLQRYKEL QDIIAILGMD ELGEEDKLVV HRARRIQFFL SQNFHVAEQF
     TGQKGSYVPV KETVQGFKEI LAGKYDHLPE DAFRLVGRIE EVVEKAKEMG VEV