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VATA_HALSA
ID   VATA_HALSA              Reviewed;         585 AA.
AC   Q9HNE3; P25163;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=VNG_2139G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1832829; DOI=10.1016/0003-9861(91)90015-b;
RA   Ihara K., Mukohata Y.;
RT   "The ATP synthase of Halobacterium salinarium (halobium) is an
RT   archaebacterial type as revealed from the amino acid sequences of its two
RT   major subunits.";
RL   Arch. Biochem. Biophys. 286:111-116(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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       (By 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG20277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X70294; CAA49775.1; -; Genomic_DNA.
DR   EMBL; AE004437; AAG20277.1; ALT_INIT; Genomic_DNA.
DR   PIR; A84364; A84364.
DR   PIR; S14732; S14732.
DR   RefSeq; WP_010903579.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNE3; -.
DR   SMR; Q9HNE3; -.
DR   STRING; 64091.VNG_2139G; -.
DR   PaxDb; Q9HNE3; -.
DR   EnsemblBacteria; AAG20277; AAG20277; VNG_2139G.
DR   GeneID; 5953572; -.
DR   GeneID; 62887437; -.
DR   KEGG; hal:VNG_2139G; -.
DR   PATRIC; fig|64091.14.peg.1637; -.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   InParanoid; Q9HNE3; -.
DR   OrthoDB; 6736at2157; -.
DR   PhylomeDB; Q9HNE3; -.
DR   BioCyc; MetaCyc:MON-681; -.
DR   Proteomes; UP000000554; 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; 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; 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   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..585
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144594"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        305
FT                   /note="A -> G (in Ref. 1; CAA49775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="W -> S (in Ref. 1; CAA49775)"
FT                   /evidence="ECO:0000305"
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
 
 
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