VATA_BORDL
ID VATA_BORDL Reviewed; 576 AA.
AC B5RLG8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=BDU_97;
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=412419;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00309};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR EMBL; CP000976; ACH93053.1; -; Genomic_DNA.
DR RefSeq; WP_012537865.1; NC_011229.1.
DR AlphaFoldDB; B5RLG8; -.
DR SMR; B5RLG8; -.
DR STRING; 412419.BDU_97; -.
DR EnsemblBacteria; ACH93053; ACH93053; BDU_97.
DR KEGG; bdu:BDU_97; -.
DR eggNOG; COG1155; Bacteria.
DR HOGENOM; CLU_008162_1_1_12; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000611; Chromosome.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR43607; 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; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..576
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000115631"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 576 AA; 63858 MW; FD3E74B7C1096DDE CRC64;
MEAKGKVVGV IGNLVTIEMV GTVSMNEIVF IKTGGQSLKA EIIRIRDGEV DAQVFEMTRG
IAVGDDVEFT DKLLTVELGP GLLSQVYDGL QNPLPELATK CGFFLERGLY LSALDRNKKW
SFNATAKVGD FVVAGDFLGF VIEGTINHQI MVPFDRRDSY RIIEIVGDGD YTVDDKIAVI
EDDAGGKHII TMSFHWPVKV PVTSYKKRLI PNETMVTQTR IIDTFFPVAK GGTFCIPGPF
GAGKTVLQQV TSRNADVDIV IIAACGERAG EVVETLKEFP ELTDPRTGKS LMERTCIICN
TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGDEAF
PAYLESVIAS FYERAGVVVL NNGSVGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
RERSDARKFP AINPLDSWSK YRGVVEYEAT EYARAFLVKG NEVNQMMRVV GEDGVSIDDF
VVYLKSELLD SCYLQQNSFD SVDAAVSFER QNYMFNILYK ILQSDFKFEN KLEARSFIND
LRQNILDMNL APFKQEKFNK LEINLKNLLR SKKLDF