ID   VATA_DEIDV              Reviewed;         582 AA.
AC   C1CXU3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Deide_00990;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO44899.1; -; Genomic_DNA.
DR   RefSeq; WP_012692022.1; NC_012526.1.
DR   AlphaFoldDB; C1CXU3; -.
DR   SMR; C1CXU3; -.
DR   STRING; 546414.Deide_00990; -.
DR   PaxDb; C1CXU3; -.
DR   PRIDE; C1CXU3; -.
DR   EnsemblBacteria; ACO44899; ACO44899; Deide_00990.
DR   KEGG; ddr:Deide_00990; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_0; -.
DR   OMA; TAFVQVY; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002208; 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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..582
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000205031"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   582 AA;  63484 MW;  F0208F96107C951C CRC64;
     MTQNKQGVVQ SIAGPAVIAD GMYGAKMYDI VRVGRERLVG EIIRLDGNTA FVQVYEDTSG
     LTVGEPVETT NLPLSVELGP GMLNGIYDGI QRPLDKIREA SGDFIARGIE VSSLDRTKKW
     AFTPSVQPGD TVVGSGILGT VPEFSFTHKI LTPPDKGGKL RWVAAAGEYT IDDTIAELED
     GTKLRLAHYW PVRAPRPVQK KLDPSLPFLT GMRILDVLFP LVMGGAAAIP GPFGSGKTVT
     QQSVAKYGNA DIVVYVGCGE RGNEMTDVLV EFPELVDPKT GGPLMHRTIL IANTSNMPVA
     AREASVYTGI TLAEYFRDQG YSVSLMADST SRWAEALREI SSRLEEMPAE EGYPPYLGAK
     LAAFYERAGA VKTLSGDDGA VSVIGAVSPA GGDMSEPVTQ ATLRITGAFW RLDAGLARRR
     HFPAINWNGS YSLFTPILDK WYRQNVGPDF PELRQRITNL LQQEAALQEV VQLVGPDALQ
     DNERLIIETG RMLRQDFLQQ NGFDPVDASA SMPKNYGLMK MFLKFYDEAD LALKNGSTID
     EIIQNPVIEK LARARYTPEN EFAAYGEGVM DQLSTTFKGV KA