ID   ATPA_BACLD              Reviewed;         502 AA.
AC   Q65DX2; Q62PE3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {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};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
GN   OrderedLocusNames=BLi03928, BL03998;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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_01346};
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_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR   EMBL; AE017333; AAU42742.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU25368.1; -; Genomic_DNA.
DR   RefSeq; WP_003186010.1; NC_006322.1.
DR   AlphaFoldDB; Q65DX2; -.
DR   SMR; Q65DX2; -.
DR   STRING; 279010.BL03998; -.
DR   PRIDE; Q65DX2; -.
DR   EnsemblBacteria; AAU25368; AAU25368; BL03998.
DR   GeneID; 66214125; -.
DR   KEGG; bld:BLi03928; -.
DR   KEGG; bli:BL03998; -.
DR   PATRIC; fig|279010.13.peg.3997; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_9; -.
DR   OMA; LQAPGVM; -.
DR   OrthoDB; 837522at2; -.
DR   BioCyc; BLIC279010:BLI_RS19300-MON; -.
DR   Proteomes; UP000000606; 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-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   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 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_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
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   3: Inferred from homology;
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..502
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000238197"
FT   REGION          117..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            362
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   502 AA;  54724 MW;  3B091FFB93506696 CRC64;
     MSIKAEEIST LIKQQIENYQ SEIEVHDVGT VIQVGDGIAR VHGLDNCMAG ELVEFSNGVL
     GLAQNLEESN VGIVILGPYK DIREGDEVKR TGRIMEVPVG EELLGRVVNP LGQPVDGMGP
     VLTSKTRPIE SPAPGVMDRK SVHEPLQTGI KSIDALIPIG RGQRELIIGD RQTGKTSIAI
     DTILNQKDQD MICIYVAIGQ KESTVRGVVE TLRKHGALDY TIVVTASASQ PAPLLYLAPY
     AGVAMGEEFM YNGKHVLVVY DDLSKQATAY RELSLLLRRP PGREAFPGDV FYLHSRLLER
     AAKLSDAKGG GSLTALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAVNPG
     LSVSRVGGSA QIKAMKKVAG TLRLDLASYR ELEAFAQFGS DLDKATQAKL NRGARTVEVL
     KQDLHKPLRV EKQVAILYAL TRGFLDDVPV EDIKRFEEEL FMYLDQNHKD LLDSIAQTGN
     LPADEDMKGA IEGFKRTFAP SN