ID VATA_METJA Reviewed; 587 AA.
AC Q57670;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 27-NOV-2024, entry version 142.
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=MJ0217;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
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=AAB98200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98200.1; ALT_INIT; Genomic_DNA.
DR PIR; B64327; B64327.
DR RefSeq; WP_064496424.1; NC_000909.1.
DR AlphaFoldDB; Q57670; -.
DR SMR; Q57670; -.
DR STRING; 243232.MJ_0217; -.
DR PaxDb; 243232-MJ_0217; -.
DR EnsemblBacteria; AAB98200; AAB98200; MJ_0217.
DR GeneID; 1451067; -.
DR KEGG; mja:MJ_0217; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR InParanoid; Q57670; -.
DR OrthoDB; 115235at2157; -.
DR PhylomeDB; Q57670; -.
DR Proteomes; UP000000805; 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 FunFam; 1.10.1140.10:FF:000002; V-type proton ATPase catalytic subunit A; 1.
DR FunFam; 2.40.30.20:FF:000002; V-type proton ATPase catalytic subunit A; 1.
DR FunFam; 2.40.50.100:FF:000008; V-type proton ATPase catalytic subunit 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; IPR055190; ATP-synt_VA_C.
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 Pfam; PF22919; ATP-synt_VA_C; 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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..587
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144599"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 587 AA; 65557 MW; 26BDD64E6D7FEEC5 CRC64;
MPVVGKIIKI AGPVVVAEGM KGAQMYEVVK VGEEKLTGEI IQLHDDKAVI QVYEETSGIK
PGEPVVGTGA PLSVELGPGM LRAMYDGIQR PLTAIEEKTG SIFIPRGVDV PALPRDIKWE
FKPVVNEGDY VEEGDIIGTV DETPSIVHKI LVPIGVKGKI VEIKEGKFTV EETVAVVETE
NGERKEITMM QKWPVRKPRP YKEKLPPEIP LITGQRVEDT FFTLAKGGTA AIPGPFGSGK
TVTQHQLAKW SDADVVVYIG CGERGNEMTE VIEEFPHLED IRTGNKLMDR TVLIANTSNM
PVAAREASVY TGITIAEYFR DMGYGVLLTA DSTSRWAEAM REISGRLEEM PGEEGYPAYL
ASRLAQFYER AGRVITLGKD NRQGFVCIVG AVSPPGGDFS EPVTSNTLRI VKVFWALDAN
LARRRHFPAI NWLQSYSLYI DDVTEWWNTN TGPDWRQLRD EAMSLLQKEA ELQEIVQLVG
PDALPDRERV ILEVARMLRE DFLQQDAFDE VDTYCPPMKQ YLMLKIIMTF YQEALKAVER
GVEPAKILGV SVKQDIARMK YIPHDEFINV KSKEIMEKIK NELGSLN
//