ID A0A1Y3GI63_9EURY Unreviewed; 590 AA.
AC A0A1Y3GI63;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=AMET1_0777 {ECO:0000313|EMBL:OUJ19125.1};
OS Methanonatronarchaeum thermophilum.
OC Archaea; Euryarchaeota; Methanonatronarchaeia; Methanonatronarchaeales;
OC Methanonatronarchaeaceae; Methanonatronarchaeum.
OX NCBI_TaxID=1927129 {ECO:0000313|EMBL:OUJ19125.1, ECO:0000313|Proteomes:UP000195137};
RN [1] {ECO:0000313|EMBL:OUJ19125.1, ECO:0000313|Proteomes:UP000195137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMET1 {ECO:0000313|EMBL:OUJ19125.1};
RA Sorokin D.Y., Makarova K.S., Abbas B., Ferrer M., Golyshin P.N.;
RT "Discovery of methanogenic haloarchaea.";
RL Submitted (DEC-2016) 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:OUJ19125.1}.
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DR EMBL; MRZU01000003; OUJ19125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3GI63; -.
DR OrthoDB; 115235at2157; -.
DR Proteomes; UP000195137; Unassembled WGS sequence.
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 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; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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; 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; 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|HAMAP-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};
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 10..72
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 88..207
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 216..436
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 590 AA; 66486 MW; 7FA8E4FEED39D942 CRC64;
MESSGEEGRI IKVSGPVVEA DNMKGTEMHE VVEIGEMGLF GEVIELDGDK AVIQCYEETS
GVAPGEKVVN TGQPLSVDLA PGLMSSIFDG IQRPLNYIRE EGGDFIPRGI EVPSVDYEKE
WKFTPEVSEG DEVGELDILG TVPETKIVEH RVMVPRGTQG VVKTIKEGEF TVDETIAEIE
TPEGEVIEIQ MLRRWPVREP RPQDEKLNPN EPLITGQRVL DTFFPMTKGG TAAIPGGFGT
GKTVLQHQVS KWADADVIIF IGCGERGNEM AEVLEEFPAL EDPETGESLM ERTILIANTS
NMPVAARESS IYTGITLAEY YRDMGYNVAL QADSTSRWAE ALREISGRLE EMPGEEGYPA
YLATRLAEFY ERAGMVRQQD RTGSVSVVGA VSPPGGDFSE PVTQNTLRIV KVFWALSTEL
KDRRHFPAID WLESYSLYNE DVKKWWDQEI KDGWLELRRR SLELLQQEDE LQEVVQLVGP
DALPEKERVV LDVSRILRED FLQQNAFHDI DTYCSPKKQM DMIETILQFY DVASEAVDQG
VPADKIAEME VKQRIARMKE VPEDEFEQEL TDIRNQMKNE VDKLKKEVRR
//
