ID   VATA_STRGC              Reviewed;         596 AA.
AC   A8AUJ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=SGO_0135;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09814.1; -; Genomic_DNA.
DR   RefSeq; WP_011999681.1; NC_009785.1.
DR   AlphaFoldDB; A8AUJ7; -.
DR   SMR; A8AUJ7; -.
DR   STRING; 467705.SGO_0135; -.
DR   EnsemblBacteria; ABV09814; ABV09814; SGO_0135.
DR   KEGG; sgo:SGO_0135; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000001131; 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; 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.
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..596
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000079066"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   596 AA;  65670 MW;  2AF72F6037173D75 CRC64;
     MSQGKIIKVS GPLVLASGMQ EANIQDICRV GDLGLIGEII EMRRDQASIQ VYEETSGLGP
     GEPVITTGSP LSVELGPGLI SQMFDGIQRP LERFQTITES DFLVRGVQLP NLDRETKWNF
     VPSLSVGDAV EAGDILGTVQ ETNLVEHRIM VPVGVSGRLA NISAGSFTVE ETVYEIEQAE
     GSIFKGTLMQ KWPVRRGRPF AQKLIPVEPL VTGQRVIDTF FPVTKGGAAA VPGPFGAGKT
     VVQHQVAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP STGQSIMQRT VLIANTSNMP
     VAAREASIYT GITIAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLEEMP GDEGYPAYLG
     SRIAEYYERA GRVKTLGSTA REGSITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAQL
     AQRRHFPAIN WLSSYSLYLD EVGAYIDQHE KIAWAEKVTK AMNILQKESE LQEIVRLVGL
     DSLSEKDRLT MNAAKMIRED YLQQNAFDDV DTYTSFKKQV ALLSNILTFD AEANRALELG
     AYFREIMEGT VELRDRIARS KFVHEDQLEK IQALSQTIEE TLHQILAQGG LDNERH