VATA_DESSY
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 03-AUG-2022, entry version 102.
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; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus; unclassified 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: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_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