ID   VATA_TREDE              Reviewed;         589 AA.
AC   Q73M28;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=TDE_1683;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12198.1; -; Genomic_DNA.
DR   RefSeq; NP_972287.1; NC_002967.9.
DR   RefSeq; WP_002669362.1; NC_002967.9.
DR   AlphaFoldDB; Q73M28; -.
DR   SMR; Q73M28; -.
DR   STRING; 243275.TDE_1683; -.
DR   PRIDE; Q73M28; -.
DR   EnsemblBacteria; AAS12198; AAS12198; TDE_1683.
DR   GeneID; 2740138; -.
DR   KEGG; tde:TDE_1683; -.
DR   PATRIC; fig|243275.7.peg.1610; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_1_1_12; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000008212; 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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..589
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000059361"
FT   BINDING         239..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   589 AA;  65263 MW;  D86E649B38F36992 CRC64;
     MTKTKGKVVG INGNMISVSF EGLVTLNEVG YVEVGSKKLK SEVIRIRGEV AQLQVFEITK
     GIKVGDIVEF TGDLLSVELG PGLLGQVYDG LQNPLPELAE QAGYFLERGI YLNALSRTAK
     WHFTPSAKEG DTLKRADLLG TVPEGSFTHR IMIPFNMYGT YKLKSIKPEG DYTVDDTIAE
     VTDERGNVIP LTMSFKWPVK RAIDCYAERL KPTETLVTKM RTMDTFFPVA KGGTYCIPGP
     FGAGKTVLQH ATSRNADVDI VIIAACGERA GEVVETLTEF PELKDPKTGR TLMERTIIIC
     NTSSMPVAAR EASVYTGVTL AEYYRQMGLD VLLLADSTSR WAQALREMSG RLEEIPGEEA
     FPAYLESYIA AFYERAGIVR LSDGSKGSVT IGGTVSPAGG NFEEPVTQAT LKVVGAFHGL
     SRERSDARKY PAIHPLDSWS KYPSVLPLEQ VKYGRSFLRR GTEVEQMMKV VGEEGTSIED
     FIIYLKGDLL DAVYLQQNSF DKVDDAVSVE RQQHIYNILI EILGTSFKFV SKDEARSYFS
     KLKLMFIDYN YSPWGSDAFK SHEDGIKKHI AEKADSLDER AKKLLKQAV