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 24-JAN-2024, entry version 137.
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; Halobacterium salinarum NRC-34001.
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; 64091-VNG_2139G; -.
DR GeneID; 68694706; -.
DR KEGG; hal:VNG_2139G; -.
DR PATRIC; fig|64091.14.peg.1637; -.
DR HOGENOM; CLU_008162_3_1_2; -.
DR InParanoid; Q9HNE3; -.
DR OrthoDB; 115235at2157; -.
DR PhylomeDB; Q9HNE3; -.
DR BioCyc; MetaCyc:MONOMER-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 CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01043; ATP_syn_A_arch; 1.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
