ID   VATA_STRP1              Reviewed;         591 AA.
AC   Q9A1Q3; Q491G8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; Synonyms=ntpA;
GN   OrderedLocusNames=SPy_0154, M5005_Spy0131;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type alpha chain is a catalytic subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR   EMBL; AE004092; AAK33257.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ50750.1; -; Genomic_DNA.
DR   RefSeq; NP_268536.1; NC_002737.2.
DR   AlphaFoldDB; Q9A1Q3; -.
DR   SMR; Q9A1Q3; -.
DR   STRING; 1314.HKU360_00177; -.
DR   PaxDb; Q9A1Q3; -.
DR   EnsemblBacteria; AAK33257; AAK33257; SPy_0154.
DR   KEGG; spy:SPy_0154; -.
DR   KEGG; spz:M5005_Spy0131; -.
DR   PATRIC; fig|160490.10.peg.135; -.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
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   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..591
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144615"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   591 AA;  64967 MW;  DBF74909A6964961 CRC64;
     MNQGKIITVS GPLVVASGMQ EANIQDICRV GHLGLVGEII EMRRDQASIQ VYEETSGIGP
     GEPVVTTGCP LSVELGPGLI SEMFDGIQRP LDRFQKATDS DFLIRGVAIP SLDRKAKWAF
     IPKLSVGQEV VAGDILGTVQ ETAVIEHRIM VPYKVSGTLV AIHAGDFTVT DTVYEIKQED
     GSIYQGSLMQ TWPVRQSRPV AQKLIPVEPL VTGQRVIDTF FPVTKGGAAA VPGPFGAGKT
     VVQHQIAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP NTGQSIMERT VLIANTSNMP
     VAAREASIYT GITIAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLQEMP GDEGYPAYLG
     SRIAEYYERA GRVRTLGSQE REGTITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAPL
     AQRRHFPAIN WLTSYSLYQD DVGSYIDRKQ QSNWSNKVTR AMAILQREAS LEEIVRLVGL
     DSLSEQDRLT MAVARQIRED YLQQNAFDSV DTFTSFPKQE AMLTNILTFN EEASKALSLG
     AYFNEIMEGT AQVRDRIARS KFIPEENLEQ IKGLTQKVTK EIHHVLAKGG I