ID   VATA_STRPI              Reviewed;         591 AA.
AC   B1ICC9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SPH_1459;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000936; ACA36749.1; -; Genomic_DNA.
DR   RefSeq; WP_000191788.1; NC_010380.1.
DR   AlphaFoldDB; B1ICC9; -.
DR   SMR; B1ICC9; -.
DR   EnsemblBacteria; ACA36749; ACA36749; SPH_1459.
DR   GeneID; 66806450; -.
DR   KEGG; spv:SPH_1459; -.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000002163; 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; Translocase; Transport.
FT   CHAIN           1..591
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000115644"
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;  65356 MW;  D535A67DBABAE684 CRC64;
     MTQGKIIKVS GPLVIASGMQ EANIQDICRV GKLGLIGEII EMRRDQASIQ VYEETSGLGP
     GEPVVTTGEP LSVELGPGLI SQMFDGIQRP LDRFKLATHN DFLVRGVEVP SLDRDIKWHF
     DSTISIGQKV STGDILGTVK ETEVVNHKIM VPYGISGEVV SIASGDFTID EVVYEIKKLD
     GSFYKGTLMQ KWPVRKARPV SKRLIPEEPL ITGQRVIDTF FPVTKGGAAA VPGPFGAGKT
     VVQHQVAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP NTGQSIMQRT VLIANTSNMP
     VAAREASIYT GITMAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLEEMP GDEGYPAYLG
     SRIAEYYERA GRSQALGLPE REGTITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAPL
     AQRRHFPAIN WLTSYSLYKD SVGTYIDDKE KTDWNSKITR AMNYLQRESS LEEIVRLVGI
     DSLSENERLT MEIAKQIRED YLQQNAFDSV DTFTSFAKQE AMLSNILTFA DQANHALELG
     SYFTEIIEGT VAVRDRMARS KYVSEDRLDE IKIISNEITH QIQLILETGG L