ID   VATA_STRSV              Reviewed;         596 AA.
AC   A3CK48;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
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=SSA_0091;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN43553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000387; ABN43553.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001034103.1; NC_009009.1.
DR   AlphaFoldDB; A3CK48; -.
DR   SMR; A3CK48; -.
DR   STRING; 388919.SSA_0091; -.
DR   EnsemblBacteria; ABN43553; ABN43553; SSA_0091.
DR   KEGG; ssa:SSA_0091; -.
DR   PATRIC; fig|388919.9.peg.85; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002148; 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_0000322469"
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;  65466 MW;  AC3DF9F722C7842A CRC64;
     MSQGKIIKVS GPLVLASGMQ EANIQDICRV GDLGLIGEII EMRRDQASIQ VYEETSGLGP
     GEPVITTGSP LSVELGPGLI SQMFDGIQRP LERFQTITAS DFLVRGVQLP NLDREAKWDF
     VPGLSVGDAV EAGDVLGTVQ ETNLVEHRIM VPVGVSGRLA NISAGSFTVE ETVYEIEQAD
     GSVFKGTLMQ KWPVRRGRPF AQKLIPVEPL VTGQRVIDTF FPVTKGGAAA VPGPFGAGKT
     VVQHQVAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP TTGQSIMQRT 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 KFIHEDQLGK IQALSQTIEE TLHQILAQGG LDNERH