ID   VATA2_TREPA             Reviewed;         605 AA.
AC   O83541;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=V-type ATP synthase alpha chain 2;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A 2;
GN   Name=atpA2; OrderedLocusNames=TP_0529;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AE000520; AAC65516.1; -; Genomic_DNA.
DR   PIR; C71313; C71313.
DR   RefSeq; WP_010881977.1; NC_021490.2.
DR   AlphaFoldDB; O83541; -.
DR   SMR; O83541; -.
DR   STRING; 243276.TPANIC_0529; -.
DR   TCDB; 3.A.2.3.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblBacteria; AAC65516; AAC65516; TP_0529.
DR   KEGG; tpa:TP_0529; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_12; -.
DR   OMA; TAFVQVY; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000000811; 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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..605
FT                   /note="V-type ATP synthase alpha chain 2"
FT                   /id="PRO_0000144621"
FT   BINDING         242..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   605 AA;  66740 MW;  65A2CB82B3822EE6 CRC64;
     MIKDDVVTGR VVRVSGPIVY AEGLSACSVY DVVDVGEASL IGEIIRLDES KAVVQVYEDD
     TGMRVGEKVT SLRRPLSVRL GPGLIGTIYD GIQRPLERLF QEDGAFLRPG ARSQPLDGSV
     RWDFRPHCNE RGEALCAGIP IAPGSVLGTV QETPSVVHTI MVPPDIRGSV LSSFKGAGAY
     TIDEEIGRTD LGEPLFLSQY WPVRRARPFS KKLAVCEPLV TGQRAIDVFF PLSKGGTAAI
     PGGFGTGKTM TQHAVAKWCD ADIIVYIGCG ERGNEMTDVL SEFPKLIDPR TGRSLMERTI
     LIANTSNMPV SAREVSLYSG ITLAEYYRDM GMHVAIMADS TSRWAEALRE LSGRMEEMPA
     EEGFPAYLPT RLAEFYERAG RVETCVAREG SVSIIGAVSP LGGDFSEPVT QHTKRFIRCF
     WALDRELAHA RHYPAIGWID SYSEYAQEVS AWWSKYDPRA GALRAAALDL LRKEQRLQQI
     VRLVGPDALP GEDRLVLMVC EMIKGGFLQQ NAFDPTDVFS CPEKQVQILR TIVDFHERAV
     VLLRAGISLS ALSQLSCREL IVRMKTTYGN EDVHKMQKVY DTMCTEFDQL SVCAAARTQG
     GEKVE