ID A0A0V8RVS5_PYROC Unreviewed; 602 AA.
AC A0A0V8RVS5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|ARBA:ARBA00018003, ECO:0000256|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473, ECO:0000256|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|ARBA:ARBA00031719, ECO:0000256|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN ORFNames=CF15_05250 {ECO:0000313|EMBL:KSW12169.1};
OS Pyrodictium occultum.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=2309 {ECO:0000313|EMBL:KSW12169.1, ECO:0000313|Proteomes:UP000053352};
RN [1] {ECO:0000313|EMBL:KSW12169.1, ECO:0000313|Proteomes:UP000053352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL-19 {ECO:0000313|EMBL:KSW12169.1,
RC ECO:0000313|Proteomes:UP000053352};
RA Utturkar S., Huber H., Leptihn S., Brown S., Stetter K.O., Podar M.;
RT "Genome sequence of Pyrodictium occultum PL-19, a marine hyperthermophilic
RT archaeon isolated from Volcano, Italy.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-Rule:MF_00309}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00309};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00309}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KSW12169.1}.
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DR EMBL; LNTB01000001; KSW12169.1; -; Genomic_DNA.
DR RefSeq; WP_058370850.1; NZ_LNTB01000001.1.
DR AlphaFoldDB; A0A0V8RVS5; -.
DR STRING; 2309.CF15_05250; -.
DR OrthoDB; 115235at2157; -.
DR Proteomes; UP000053352; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00309};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Reference proteome {ECO:0000313|Proteomes:UP000053352};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00309}.
FT DOMAIN 228..422
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 602 AA; 67382 MW; EB0E2909F10FF6B1 CRC64;
MPVKGRIIRV AGPLVVAEGM QGVQMYEMVE VGEERLVGEV NRIVGDKAYI QVYETTTGIK
PGEPVYGTGA PLSVELGPGL IGRIYDGIQR PLDAIRDQTK SIFIRRGVKV PALDRGRKWS
FKPSGLRPGD KVSGGDVLGE VPETSLVTHR VLVPPGVHGV LRWIASEGEY TVEDTIAEVE
AGDDRKFEIK LYHRWPVRRP RPVVEKMDPV EPLITGLRVI DTMFPMAKGG TGAIPGPFGS
GKTVTLQSLA KWSSAKIVIY IGCGERGNEM TEVLETFPEL QDPWTGKPMM ERTILIANTS
NMPVAAREAS IYTGITMAEY YRDMGYDVLL VADSTSRWAE ALREIAGRLE EMPAEEGYPS
YLASRLAEFY SRAGRVRVPG KPERVGSVTV VGAVSPPGGD FTEPVTANTK RFIRVFWALD
AKLAYSRHYP AINWLLSYSA YVETVAKWWH ENISPKWLEY RNTAYELLLR EDELREIVRL
VGTEGLSEKD KLVLEVARII REGFLQQNAF DKIDAFATPQ KQWKQLETII DFYKAALDAL
DHGMTVKEIR EKLADKIREF IMARFNVPND RLEELDRIKQ ELLKGLEELM EQRGSLAAAP
TA
//
