VATA_THEKO
ID VATA_THEKO Reviewed; 585 AA.
AC Q5JIR3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=TK1602;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00309};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_00309}.
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; AP006878; BAD85791.1; -; Genomic_DNA.
DR RefSeq; WP_011250553.1; NC_006624.1.
DR AlphaFoldDB; Q5JIR3; -.
DR SMR; Q5JIR3; -.
DR STRING; 69014.TK1602; -.
DR EnsemblBacteria; BAD85791; BAD85791; TK1602.
DR GeneID; 3235294; -.
DR KEGG; tko:TK1602; -.
DR PATRIC; fig|69014.16.peg.1561; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR InParanoid; Q5JIR3; -.
DR OMA; TAFVQVY; -.
DR OrthoDB; 6736at2157; -.
DR PhylomeDB; Q5JIR3; -.
DR Proteomes; UP000000536; 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; 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; Reference proteome; Translocase; Transport.
FT CHAIN 1..585
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144604"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 585 AA; 65437 MW; A0627C552AB278FC CRC64;
MGRIIRVTGP LVVADGMKGA KMYEVVRVGE IGLIGEIIRL EGDKAVIQVY EETAGIRPGE
PVEGTGSSLS VELGPGLLTA MYDGIQRPLE VLRQLSGDFI ARGLTAPALP RDKKWHFTPK
VKVGDKVVGG DVLGVVPETS IIEHKILVPP WVEGEIVEIA EEGDYTVEEV IAKVKKPDGT
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 RSYSLYIDAI QDWWHKNVDP EWRKMRDTAM ALLQKEAELQ EIVRIVGPDA
LPDREKAILI VTRMLREDYL QQDAFDEVDT YCPPKKQVTM MRVILNFYEK TMQAVDRGVP
VDEIAKLPVR EKIGRMKFEP DVEKVRALID ETNQQFEELF KKYGA