ID   VATA_HALS3              Reviewed;         585 AA.
AC   B0R755;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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=OE_3985R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR   EMBL; AM774415; CAP14574.1; -; Genomic_DNA.
DR   RefSeq; WP_010903579.1; NC_010364.1.
DR   AlphaFoldDB; B0R755; -.
DR   SMR; B0R755; -.
DR   PRIDE; B0R755; -.
DR   EnsemblBacteria; CAP14574; CAP14574; OE_3985R.
DR   GeneID; 5953572; -.
DR   GeneID; 62887437; -.
DR   KEGG; hsl:OE_3985R; -.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   PhylomeDB; B0R755; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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; IPR005726; ATP_synth_asu_arc.
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   TIGRFAMs; TIGR01043; ATP_syn_A_arch; 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..585
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000115640"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   585 AA;  64218 MW;  A8FE534DEEF99734 CRC64;
     MSQAEAITDT GEIESVSGPV VTATGLDAQM NDVVYVGDEG LMGEVIEIEG DVTTIQVYEE
     TSGIGPGQPV DNTGEPLTVD LGPGMLDSIY DGVQRPLDVL EDEMGAFLDR GVDAPGIDLD
     TDWEFEPTVE AGDEVAAGDV VGTVDETVSI EHKVLVPPRS DGGEVVAVES GTFTVDDTVV
     ELDTGEEIQM HQEWPVRRQR PTVDKQTPTE PLVSGQRILD GLFPIAKGGT AAIPGPFGSG
     KTVTQQSLAK FADADIVVYI GCGERGNEMT EVIEDFPELP DPQTGNPLMA RTTLIANTSN
     MPVAARESCI YTGITIAEYY RDMGYDVALM ADSTSRWAEA MREISSRLEE MPGEEGYPAY
     LAARLSEFYE RAGYFENFNG TEGSISVIGA VSPPGGDFSE PVTQNTLRIV KTFWALDSDL
     AERRHFPAIN WDESYSLYKD QLDPWFTDNV VDDWAEQRQW AVDILDEESE LEEIVQLVGK
     DALPEDQQLT LEVARYIREA WLQQNALHDV DRYCPPEKTY AILSGIKTLH EESFEALDAG
     VPVEEITSID AAPRLNRLGT TPDDEHEAEV AEIKQQITEQ LRELY