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Database: UniProt
Entry: O06504
LinkDB: O06504
Original site: O06504 
ID   VATA_DESSY              Reviewed;         585 AA.
AC   O06504;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-NOV-2023, entry version 107.
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;
OS   Desulfurococcus sp. (strain SY).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=59822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SY;
RX   PubMed=9177272; DOI=10.1006/bbrc.1997.6644;
RA   Shibui H., Hamamoto T., Yohda M., Kagawa Y.;
RT   "The stabilizing residues and the functional domains in the
RT   hyperthermophilic V-ATPase of Desulfurococcus.";
RL   Biochem. Biophys. Res. Commun. 234:341-345(1997).
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   -!- 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}.
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DR   EMBL; U96487; AAB64416.1; -; Genomic_DNA.
DR   PIR; T44674; T44674.
DR   AlphaFoldDB; O06504; -.
DR   SMR; O06504; -.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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; Translocase; Transport.
FT   CHAIN           1..585
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144593"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   585 AA;  65477 MW;  A63FD8E540E7D35A CRC64;
     MGRIIRVTGP LVVADGMKGS KMYEVVRVGE MGLIGEIIRL EGDKAVIQVY EETAGIRPGE
     PVEGTGSSLS VELGPGLLTS MYDGIQRPLE KLRELSGDFI ARGLTAPALP RDKKWHFTPT
     VKVGDKVTGG DILGVVPETS IIEHKILVPP WVEGEIVEIA EEGDYTVEEV IAKVKKPDGS
     IEELKMYHKW PVRVKRPYKN KLPPEVPLIT GQRTIDTFFS IAKGGTAAIP GPFGSGKTVT
     QHQLAKWSDA QVVVYIGCGE RGNEMTDVLE EFPKLKDPKT GKPLMERTVL IANTSNMPVA
     AREASIYTGI TIAEYFRDQG YDVALMADST SRWAEALREI SGRLEEMPGE EGYPAYLASK
     IAEFYERAGR VVTLGSEPRV GSVSVIGAVS PPGGDFSEPV VQNTLRVVKV FWALDADLAR
     RRHFPAINWL RSYSLYLDSI QDWWHKNVDP EWRKMRDTAM ALLQKEAELQ EIVRIVGPDA
     LPDREKAILI VTRMLREDYL QQDAFDEVDT YCPPKKQVTM MRVILNFYER TMEAVDRGVP
     VDEIAKLPVR EKIGRMKFEP DIEKIRALID ETNEQFEELF KKYGA
//
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