ID   VATA_BORT9              Reviewed;         576 AA.
AC   A1QYP3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=BT0094;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) 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: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; CP000049; AAX17435.1; -; Genomic_DNA.
DR   RefSeq; WP_011772054.1; NC_008710.1.
DR   AlphaFoldDB; A1QYP3; -.
DR   SMR; A1QYP3; -.
DR   STRING; 314724.BT0094; -.
DR   KEGG; btu:BT0094; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_1_1_12; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000001205; Chromosome.
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; 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; 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_1000132881"
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;  63679 MW;  020699B9027D6521 CRC64;
     MEARGKVVGV IGNLVTIEIV GTVSMNEIVF IKTGGRSLKA EIIRIRDGEV DAQVFEMTKG
     IAVGDDIEFT DKLLTVELGP GLLSQVYDGL QNPLSELAAQ CGFFLERGLY LSALDRSKKW
     SFNATAKVGD IVVAGDYLGF VVEGTIKHKI MVPFYRKDSY KIVEIVSDGN YTVDDKIAVI
     ENDAGGRHVI TMSFHWPVKV PITSYKDRLI PSEPMVTQTR IIDTFFPVAK GGTFCIPGPF
     GAGKTVLQQV TSRNADVDVV IIAACGERAG EVVETLKEFP ELIDPRTGKS LMDRTCIICN
     TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF
     PAYLESVIAS FYERAGIVVL NDGNVGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
     RERSDARKFP AINPLESWSK YRGVVESEKT GYARSFLAKG NEINQMMKVV GEEGISIGDF
     LVYLKSELLD ACYLQQNSFD SVDTAVSPER QNYMFDILYD ILQSDFKFEN KLEARSFVNE
     LRQNILDMNL NPFKEEKFNK LENTLKDLVR SKKLDF