ID A0A2U1B747_9BACT Unreviewed; 580 AA.
AC A0A2U1B747;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN ORFNames=C8D82_10621 {ECO:0000313|EMBL:PVY44504.1};
OS Victivallis vadensis.
OC Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC Victivallis.
OX NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY44504.1, ECO:0000313|Proteomes:UP000245959};
RN [1] {ECO:0000313|EMBL:PVY44504.1, ECO:0000313|Proteomes:UP000245959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY44504.1,
RC ECO:0000313|Proteomes:UP000245959};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type alpha chain is a catalytic subunit.
CC {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|HAMAP-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:PVY44504.1}.
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DR EMBL; QEKH01000006; PVY44504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1B747; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000245959; 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; cd01426; ATP-synt_F1_V1_A1_AB_FliI_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.30.30.650; -; 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; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245959};
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..73
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 90..212
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 223..442
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 241..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 580 AA; 64766 MW; EA7F36E11FCF5E10 CRC64;
MPEVKSTQKV VGVNGNMMTV EFTDRVMQNE VAFAKVGDTR LKCEVIRVRG NRADLQVFES
TNGLKVGDEV EFTDELLSVE LGPGLLKQVY DGLQNPLNLL AEQSGFFLKR GLYLRALDRD
VKWAFTPIAK PGDKVRPGDR IGHVPEGIIK HYIMVPLAWK GEWTLQTVAA PGEYTIDEVM
AVAVNDQGES RRITMTQFWP VKIPITDYSE KLLPERTMIT QQRTIDTFFP VAVGGTFCTP
GPFGAGKTVL QHAISRYAEA DVVIIAACGE RAGEVVEILR EFPELEDPKT GQPLINRSII
ICNTSSMPVA AREASVYTAV TLAEYYRQMG LNTLLLADST SRWAQALREM SGRLEEIPGE
EAFPAYLESL IASFYERAGL VRLRTGEEGS VTIGGAVSPA GGNFEEPVTQ ATLKVVGAFL
GLSRERSDAR RYPAIHPLDS WSKYRSVVDR KELDYARGIL RQGSEVNQMM KVIGEEGTSL
DDFVVYLKSE FLDYVYLQQN TFDAVDGATG AERQRYMFDR ISKVLEGSFT LPDKDTARRY
FLELRQMFMD LNYLPMDSEE FKRQEAGIEA KIAERSSANA
//
