VATA_THESI
ID VATA_THESI Reviewed; 585 AA.
AC O32466;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Thermococcus sp. (strain KI).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus; unclassified Thermococcus.
OX NCBI_TaxID=269443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9370240; DOI=10.1016/s0005-2736(97)00138-7;
RA Iida T., Kanai S., Inatomi K., Kamagata Y., Maruyama T.;
RT "Alpha- and beta-subunits of a V-type membrane ATPase in a
RT hyperthermophilic sulfur-dependent archaeum, Thermococcus sp. KI.";
RL Biochim. Biophys. Acta 1329:12-17(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; D88772; BAA23342.1; -; Genomic_DNA.
DR PIR; T44309; T44309.
DR AlphaFoldDB; O32466; -.
DR SMR; O32466; -.
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; 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 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 SMART; SM00382; AAA; 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_0000144608"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 65485 MW; B1653C8AC2F25054 CRC64;
MGRIIRVTGP LVVADGMKGA KMYEVVRVGE MGLIGEIIRL EGDKAVIQVY EETAGIRPGE
PVEGTGSSLS VELGPGLLTS MYDGIQRPLD VLRQLSGDFI ARGLTAPALP RDKKWHFTPK
VKVGDKVVGG DILGVVPETS IIEHKILVPP WVEGEIVEIA EEGDYTVEEV IVKVKKPDGT
IEELKMYHRW PVRVKRPYKQ KLPPEVPLIT GQRTIDTFFS QAKGGTAAIP GPFGSGKTVT
QHQLAKWSDA QVVVYIGCGE RGNEMTDVLE EFPKLKDPKT GKPLMERTVL IANTSNMPVA
AREASIYTGI TIAEYFRDQG YDVALMADST SRWAEALREI SGRLEEMPGE EGYPAYLASK
IAEFYERAGR VITLGSDERV GSVSVIGAVS PPGGDFSEPV VQNTLRVVKV FWALDADLAR
RRHFPAINWL RSYSLYVDAI QDWWHKNVDP EWRKMRDTAM ALLQKEAELQ EIVRIVGPDA
LPDREKAILI VTRMLREDYL QQDAFDEVDT YCPPKKQVTM MRVILNFYEK TMQAVDRGVP
VDEIAKLPVR EKIGRMKFEP DVEKVRALID ETNQQFEELF KKYGA