ID   VATA_IGNH4              Reviewed;         596 AA.
AC   A8AC29;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Igni_1305;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal 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   -!- INTERACTION:
CC       A8AC29; A8AAA9: atpB; NbExp=2; IntAct=EBI-15831423, EBI-15831444;
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR   EMBL; CP000816; ABU82481.1; -; Genomic_DNA.
DR   RefSeq; WP_012123445.1; NC_009776.1.
DR   AlphaFoldDB; A8AC29; -.
DR   SMR; A8AC29; -.
DR   DIP; DIP-58544N; -.
DR   IntAct; A8AC29; 1.
DR   STRING; 453591.Igni_1305; -.
DR   PRIDE; A8AC29; -.
DR   EnsemblBacteria; ABU82481; ABU82481; Igni_1305.
DR   GeneID; 5563173; -.
DR   KEGG; iho:Igni_1305; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 6736at2157; -.
DR   PhylomeDB; A8AC29; -.
DR   Proteomes; UP000000262; Chromosome.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
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_1000059344"
FT   BINDING         241..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   596 AA;  66713 MW;  B3754A4A3537EA82 CRC64;
     MAVKGKVLRV RGPVVIAEDM QGVQMYEVVE VGKDGLVGEV TRITGDKAVI QVYEDTTGIT
     PGEPVVGTGS PFSVELGPGL LSHIFDGILR PLESIHEVAK SPFIKRGIKV PSLDRSKKWE
     WRPNPELKPG DKVSGDDILG TVPETPLIEH KVMVPPNVVP VDKAATLKWL APAGEYTIED
     TIAVVEYEGK EIELKMYHRW PIRRPRPVKE KFEPVTPLIT GVRVLDTLFP MAKGGTGAIP
     GPFGSGKTVT LRTLAAWSDA KVVIYVGCGE RGNEMTDVLV NFPHYKDPWS GRPLMERTIL
     VANTSNMPVA AREASIYVGV TLAEYYRDMG YDSLLIADST SRWAEALRDI AGRMEEMPAE
     EGFPPYLASR LAEYYERAGR ARIPGRPERV GSVTIASAVS PPGGDFSEPV TSHTRRFVRV
     FWALDASLAY ARHYPAINWL VSYSLYVDTV AKWWHENISP KWKEYRDEMM SILLKEDELK
     EIVRLVGPES LSEPDKLIIE TARIIKEAFL QQNAFDPIDA FCSPKKQFLM MKIIIDFYRK
     AKELVNAGVP VATIREAVKE EVAELIRSRF TVRNEELEKL EDLYARFMEK LSSLSP