ID   VATA_BORAP              Reviewed;         575 AA.
AC   Q0SP70; G0IQT9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 105.
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};
GN   OrderedLocusNames=BAPKO_0095, BafPKo_0092;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABH01358.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000395; ABH01358.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002933; AEL69325.1; -; Genomic_DNA.
DR   RefSeq; WP_004790162.1; NC_017238.1.
DR   AlphaFoldDB; Q0SP70; -.
DR   SMR; Q0SP70; -.
DR   STRING; 390236.BafPKo_0092; -.
DR   EnsemblBacteria; AEL69325; AEL69325; BafPKo_0092.
DR   KEGG; baf:BAPKO_0095; -.
DR   KEGG; bafz:BafPKo_0092; -.
DR   PATRIC; fig|390236.22.peg.91; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_1_1_12; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000005216; 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_0000322459"
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;  64012 MW;  E9490CCEECF42497 CRC64;
     MNTKGKVVGV NGNLVTIEVE GSVSMNEVLF VKTGGRNLKA EVIRVRGNEV DAQVFELTKG
     ISVGDLVEFT DKLLTVELGP GLLTQVYDGL QNPLPELAIK CGFFLERGVY LRPLNKDKKW
     NFKKTSKVGD SVIAGDFLGF VIEGTVHHQI MIPFYKRDSY KIVEIVNDGD YSIDEQIAVI
     EDDSGMRHSI TMSFHWPVKI PITNYKQRLI PSEPMLTQTR IIDTFFPVAK GGTFCIPGPF
     GAGKTVLQQV TSRNADVDIV IIAACGERAG EVVETLKEFP ELIDPKTGKS LMDRTCIICN
     TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF
     PAYLESVIAS FYERAGIVVL NNGDIGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
     RERSDARKFP AISPLESWSK YKGVIDSKKT EYVRSFLVKG NEINQMMKVV GEEGISNEDF
     LIYLKSELLD SCYLQQNSFD SIDAAVNSER QNYMFDIVYN ILKTNFEFSD KLQARDFINE
     LRQNLLDMNL SSFKDSKFNK LEHTLSELVN FKKVI