Entry sw:ATPA_BACSU

ID   ATPA_BACSU              Reviewed;         502 AA.
AC   P37808;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   30-NOV-2016, entry version 136.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=Vegetative protein 100;
DE            Short=VEG100;
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
GN   OrderedLocusNames=BSU36830;
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;
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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 2-16.
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
RP   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).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The alpha chain is a regulatory
CC       subunit.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains (Probable). The F(1)F(0) complex
CC       interacts with SpoIIIJ and YqjG; YqgA is found in the same
CC       complex. {ECO:0000255|HAMAP-Rule:MF_01346,
CC       ECO:0000269|PubMed:19717609, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
DR   EMBL; Z28592; CAA82258.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15700.1; -; Genomic_DNA.
DR   PIR; I40366; I40366.
DR   RefSeq; NP_391564.1; NC_000964.3.
DR   RefSeq; WP_003243657.1; NZ_JNCM01000034.1.
DR   ProteinModelPortal; P37808; -.
DR   IntAct; P37808; 3.
DR   MINT; MINT-8366296; -.
DR   STRING; 224308.Bsubs1_010100019911; -.
DR   PaxDb; P37808; -.
DR   PRIDE; P37808; -.
DR   EnsemblBacteria; CAB15700; CAB15700; BSU36830.
DR   GeneID; 936995; -.
DR   KEGG; bsu:BSU36830; -.
DR   PATRIC; 18979400; VBIBacSub10457_3862.
DR   eggNOG; ENOG4105CDG; Bacteria.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   InParanoid; P37808; -.
DR   KO; K02111; -.
DR   OMA; QVVSIWA; -.
DR   PhylomeDB; P37808; -.
DR   BioCyc; BSUB:BSU36830-MONOMER; -.
DR   SABIO-RK; P37808; -.
DR   Proteomes; UP000001570; 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); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR15184:SF3; PTHR15184:SF3; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome;
KW   Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW   Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW   Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:9298659}.
FT   CHAIN         2    502       ATP synthase subunit alpha.
FT                                /FTId=PRO_0000144319.
FT   NP_BIND     169    176       ATP. {ECO:0000255|HAMAP-Rule:MF_01346}.
FT   SITE        362    362       Required for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       149    364       ipfam:ATP-synt_ab [T]
FT   MYHIT        25     92       ipfam:ATP-synt_ab_N [T]
FT   MYHIT         1    499       ihamap:ATP_synth_alpha_bact [T]
FT   MYHIT       371    491       ipfam:ATP-synt_ab_C [T]
FT   MYHIT       355    364       ipat:ATPASE_ALPHA_BETA [T]
SQ   SEQUENCE   502 AA;  54598 MW;  5DBBD671B37C974C CRC64;
     MSIKAEEIST LIKQQIQNYQ SDIEVQDVGT VIQVGDGIAR VHGLDNCMAG ELVEFSNGVL
     GMAQNLEESN VGIVILGPFS EIREGDEVKR TGRIMEVPVG EELIGRIVNP LGQPVDGLGP
     ILTSKTRPIE SPAPGVMDRK SVHEPLQTGI KAIDALIPIG RGQRELIIGD RQTGKTSVAI
     DAILNQKDQD MICVYVAIGQ KESTVRGVVE TLRKHGALDY TIVVTASASQ PAPLLYLAPY
     AGVTMAEEFM YNGKHVLVVY DDLSKQAAAY RELSLLLRRP PGREAFPGDV FYLHSRLLER
     AAKLSDAKGA GSITALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAINAG
     LSVSRVGGSA QIKAMKKVSG TLRLDLASYR ELEAFAQFGS DLDQATQAKL NRGARTVEVL
     KQDLNKPLPV EKQVAILYAL TKGYLDDIPV ADIRRFEEEY YMYLDQNHKD LLDGIAKTGN
     LPADEDFKAA IEGFKRTFAP SN
//