ID   VATA_BORBZ              Reviewed;         575 AA.
AC   B7J127;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BbuZS7_0094;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK74625.1; -; Genomic_DNA.
DR   RefSeq; WP_012597331.1; NC_011728.1.
DR   AlphaFoldDB; B7J127; -.
DR   SMR; B7J127; -.
DR   EnsemblBacteria; ACK74625; ACK74625; BbuZS7_0094.
DR   KEGG; bbz:BbuZS7_0094; -.
DR   HOGENOM; CLU_008162_1_1_12; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000006901; 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; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..575
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000119523"
FT   BINDING         238..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   575 AA;  64093 MW;  9E5A650CE14FE26A CRC64;
     MNTKGKVVGV NGNLVTIEVE GSVFMNEVLF VKTAGRNLKA EVIRIRGNEV DAQVFELTKG
     ISVGDLVEFT DKLLTVELGP GLLTQVYDGL QNPLPELAIQ CGFFLERGVY LRPLNKDKKW
     NFKKTSKVGD IVIAGDFLGF VIEGTVHHQI MIPFYKRDSY KIVEIVSDGD YSIDEQIAVI
     EDDSGMRHNI TMSFHWPVKV PITNYKERLI PSEPMLTQTR IIDTFFPVAK GGTFCIPGPF
     GAGKTVLQQV TSRNADVDVV IIAACGERAG EVVETLKEFP ELMDPKTGKS LMDRTCIICN
     TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF
     PAYLESVIAS FYERAGIVVL NNGDIGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
     RERSDARKFP AISPLESWSK YKGVIDQKKT EYARSFLVKG NEINQMMKVV GEEGISNDDF
     LIYLKSELLD SCYLQQNSFD SIDAAVSSER QNYMFDIVYN ILKTNFEFSD KLQARDFINE
     LRQNLLDMNL SSFKDHKFNK LEHALGELIN FKKVI