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VATA_STRPN
ID   VATA_STRPN              Reviewed;         591 AA.
AC   Q97QA8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=SP_1317;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; AE005672; AAK75415.1; -; Genomic_DNA.
DR   PIR; F95152; F95152.
DR   RefSeq; WP_000191781.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97QA8; -.
DR   SMR; Q97QA8; -.
DR   STRING; 170187.SP_1317; -.
DR   EnsemblBacteria; AAK75415; AAK75415; SP_1317.
DR   KEGG; spn:SP_1317; -.
DR   eggNOG; COG1155; Bacteria.
DR   OMA; RIVKTFW; -.
DR   PhylomeDB; Q97QA8; -.
DR   BioCyc; SPNE170187:G1FZB-1329-MON; -.
DR   Proteomes; UP000000585; 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_1000059359"
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;  65279 MW;  F8BC60A761473A65 CRC64;
     MTQGKIIKVS GPLVIASGMQ EANIQDICRV GKLGLIGEII EMRRDQASIQ VYEETSGLGP
     GEPVVTTGEP LSVELGPGLI SQMFDGIQRP LDRFKLATHN DFLVRGVEVP SLDRDIKWHF
     DSTIAIGQKV STGDILGTVK ETEVVNHKIM VPYGVSGEVV SIASGDFTID EVVYEIKKLD
     GSFYKGTLMQ KWPVRKARPV SKRLIPEEPL ITGQRVIDAF FPVTKGGAAA VPGPFGAGKT
     VVQHQVAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP NTGQSIMQRT VLIANTSNMP
     VAAREASIYT GITMAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLEEMP GDEGYPAYLG
     SRIAEYYERA GRSQVLGLPE REGTITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAPL
     AQRRHFPAIN WLTSYSLYKD SVGTYIDGKE KTDWNSKITR AMNYLQRESS LEEIVRLVGI
     DSLSDNERLT MEIAKQIRED YLQQNAFDSV DTFTSFAKQE AMLSNILTFA DQANHALELG
     SYFTEIMEGT VAVRDRMARS KYVSEDRLDE IKIISNEITH QIHLILETGG L
 
 
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