ID M0EUQ3_9EURY Unreviewed; 587 AA.
AC M0EUQ3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=C466_15499 {ECO:0000313|EMBL:ELZ50164.1};
OS Halorubrum distributum JCM 10118.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227468 {ECO:0000313|EMBL:ELZ50164.1, ECO:0000313|Proteomes:UP000011614};
RN [1] {ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|Proteomes:UP000011614};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELZ50164.1, ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|EMBL:ELZ50164.1,
RC ECO:0000313|Proteomes:UP000011614};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ50164.1}.
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; AOJN01000066; ELZ50164.1; -; Genomic_DNA.
DR RefSeq; WP_004598770.1; NZ_AOJN01000066.1.
DR AlphaFoldDB; M0EUQ3; -.
DR PATRIC; fig|1227468.4.peg.3064; -.
DR OrthoDB; 115235at2157; -.
DR Proteomes; UP000011614; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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 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 Hydrolase {ECO:0000313|EMBL:ELZ50164.1};
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 16..77
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 93..209
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 219..440
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 587 AA; 64745 MW; ABF8C561D28A8999 CRC64;
MSKADTTDAE TDNGVIQSVS GPVVTARDLN ARMNDVVYVG DEGLMGEVIE IEGDLTTVQV
YEETSGVGPG EPVENTGEPL SVDLGPGMLD AIYDGVQRPL DVLEGKMGSP YLDRGVDAPG
IDLEEKWEFE PEVEEGDVVE PGDIVGVVEE TVTIDHKVMV PPDYEGGEVV AAEAGSFDVT
ETVVELDNGE EVSMHQEWPV REARPANDKK TPRTPLVSGQ RILDGLFPIA KGGTAAIPGP
FGSGKTVTQH QLAKYADADI IVYVGCGERG NEMTEVIEDF PELEDPANGN PLMARTSLIA
NTSNMPVAAR ESCIYTGITI AEYYRDMGYD VALMADSTSR WAEAMREISS RLEEMPGEEG
YPAYLAARLA QFYERAGYFE NINGTEGSVS AIGAVSPPGG DFSEPVTQNT LRIVKTFWAL
DADLAERRHF PSINWNESYS LYKDQLDPWF EDEVADDWAE RRQWAVDVLD EETELQEIVQ
LVGKDALPDD QQLTLEVARY LREAYLQQNA FHPVDTFCPP EKTYLMLTTI QKFNDEAFDA
LDAGVPVEEI VDTEAAPRIN RIGVQEDYEE YVEDLKAEIT EELRSLY
//