ID D6GWS6_PARA5 Unreviewed; 337 AA.
AC D6GWS6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|ARBA:ARBA00018003};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|ARBA:ARBA00031719};
GN ORFNames=BJBARM5_0951 {ECO:0000313|EMBL:EFD92343.1};
OS Candidatus Parvarchaeum acidophilus ARMAN-5.
OC Archaea; Candidatus Parvarchaeota; Parvarchaeum.
OX NCBI_TaxID=662762 {ECO:0000313|EMBL:EFD92343.1, ECO:0000313|Proteomes:UP000009376};
RN [1] {ECO:0000313|EMBL:EFD92343.1, ECO:0000313|Proteomes:UP000009376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20421484; DOI=10.1073/pnas.0914470107;
RA Baker B.J., Comolli L.R., Dick G.J., Hauser L.J., Hyatt D., Dill B.D.,
RA Land M.L., Verberkmoes N.C., Hettich R.L., Banfield J.F.;
RT "Enigmatic, ultrasmall, uncultivated Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8806-8811(2010).
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 {ECO:0000256|ARBA:ARBA00003912}.
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:0000256|ARBA:ARBA00001741};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; GG745607; EFD92343.1; -; Genomic_DNA.
DR AlphaFoldDB; D6GWS6; -.
DR Proteomes; UP000009376; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009376};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..65
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 83..202
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 211..335
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 337 AA; 36689 MW; 26376135F5AFDA4D CRC64;
MEGKVIGISG SVVTVAGLKN PKMNNIVFIG EKSLVGEIVK IEKDNAIVQV YEDTSGLRVG
ETAIDSNEPL SVELGPGLIG SIFDGIQRPL DKILAKEGTF IGSGVKVDSL DREKKWHFKP
KMEVGKEVSA GEELGEVKET SLIKHRILVP VNKHGVIKSI AEEGEYTLND TIAVLENENK
KEEIKLMTKW PVRTPRPVKE KLAPNIPLLT GQRVIDTMFP IAMGGTAAVP GPFGSGKTVI
QHQLAKWSDA DVIVYVGCGE RGNEMTEILS TFPELKDPKS GKPLMDRTIL IANTSNMPVA
AREASIYTGI TLAEYYRDMG YSVAVMADST SRWAQDL
//
