VATA_BORHD
ID VATA_BORHD Reviewed; 579 AA.
AC B2S1S8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BH0094;
OS Borrelia hermsii (strain HS1 / DAH).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 / DAH;
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; CP000048; AAX16615.1; -; Genomic_DNA.
DR RefSeq; WP_012421872.1; NC_010673.1.
DR AlphaFoldDB; B2S1S8; -.
DR SMR; B2S1S8; -.
DR KEGG; bhr:BH0094; -.
DR HOGENOM; CLU_008162_1_1_12; -.
DR OMA; RIVKTFW; -.
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..579
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000115632"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 579 AA; 64154 MW; DCAC8AB8A763C7F1 CRC64;
MEARGKVVGV IGNLVTIEVV GTVSMNEIVF IKTGGRSLKA EIIRIRDGEV DAQVFEMTRG
IAVGDDIEFT NKLLTVELGP GLLSQVYDGL QNPLPELAAQ CGFFLERGLY LSALDRKKKW
HFNATAKVGD IVVAGDFLGF VIEGTIKHKI MIPFDRRDSY SIVEIVSDGD YTIDDKIAVV
ENDAGGKHII TMSFHWPVKI PITNYKERLI PSEPMVTQTR IIDTFFPVAK GGTFCIPGPF
GAGKTVLQQV TSRNADVDIV IIAACGERAG EVVETLKEFP ELIDPRTGKS LMERTCIICN
TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF
PAYLESVIAS FYERAGIVVL NDGSFGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
RERSDARKFP AINPLESWSK YRGVVEFGKT EYARDFLAKG NEINQMMKVV GEEGISNGDF
LVYLKSELLD SCYLQQNSFD SVDAAVNPER QNYMFDMLYD ILQSDFKFES KLEARGFINE
LRQNILDMNL TPFKEEKFNK LEVSLKNLVR SKKLDFRGA