ID   VATA_DEIRA              Reviewed;         582 AA.
AC   Q9RWG8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=V-type ATP synthase alpha chain;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A;
GN   Name=atpA; OrderedLocusNames=DR_0700;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF10278.1; -; Genomic_DNA.
DR   PIR; A75488; A75488.
DR   RefSeq; NP_294423.1; NC_001263.1.
DR   RefSeq; WP_010887345.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RWG8; -.
DR   SMR; Q9RWG8; -.
DR   STRING; 243230.DR_0700; -.
DR   EnsemblBacteria; AAF10278; AAF10278; DR_0700.
DR   KEGG; dra:DR_0700; -.
DR   PATRIC; fig|243230.17.peg.878; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_0; -.
DR   InParanoid; Q9RWG8; -.
DR   OMA; TAFVQVY; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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; IBA:GO_Central.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
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..582
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144614"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   582 AA;  63583 MW;  204F92787EECB2BD CRC64;
     MTQQKQGVVQ SIAGPAVIAK GMYGAKMYDI VRVGQERLVG EIIRLDGDTA FVQVYEDTAG
     LTVGEPVETT GLPLSVELGP GMLNGIYDGI QRPLDKIREA SGNFIARGIE VSSLNREQKW
     DFTPSVQAGD TVTGSGILGT VPEFSFTHKI LVPPEVQGRL RSVAPAGQYT IDDTIAELED
     GTKLRLAHYW PVRAPRPVQK KLDPSLPFLT GMRILDVMFP LVMGGAAAIP GPFGSGKTVT
     QQSVAKYGNA DIVVYVGCGE RGNEMTDVLV EFPELEDPKT GGPLMHRTIL IANTSNMPVA
     AREASVYTGV TLAEYFRDQG YSVSLMADST SRWAEALREI SSRLEEMPAE EGYPPYLGAK
     LAAFYERAGA VKTLAGEDGA VSVIGAVSPA GGDMSEPVTQ ATLRITGAFW RLDAGLARRR
     HFPAINWNGS YSLFTPILDK WYRENVGPDF PELRQRIGSL LQQEAALQEV VQLVGPDALQ
     DNERLIIETG RMLRQDFLQQ NGFDPVDASA SMPKNYGLMK MFLKFYDEAE AALRNGLTID
     EIIQNPVIEK LARARYTPEN EFMAYGEGVM DELDQTFKAV KA