ID   VATA2_CLOTE             Reviewed;         592 AA.
AC   Q891P1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=V-type ATP synthase alpha chain 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA2 {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=CTC_02328;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36804.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q891P1; -.
DR   SMR; Q891P1; -.
DR   STRING; 212717.CTC_02328; -.
DR   PRIDE; Q891P1; -.
DR   EnsemblBacteria; AAO36804; AAO36804; CTC_02328.
DR   KEGG; ctc:CTC_02328; -.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; TAFVQVY; -.
DR   Proteomes; UP000001412; 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; IPR020003; ATPase_a/bsu_AS.
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.
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..592
FT                   /note="V-type ATP synthase alpha chain 2"
FT                   /id="PRO_0000322465"
FT   BINDING         237..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   592 AA;  66792 MW;  BFC593DAE14686EC CRC64;
     MVLLDSLVGT IVGINGPVIK AEGMSKFKMR EMVMVGKKKL IGEIIILEND LATIQVYEET
     SGLKIGENIS STGMPLSLKL GPGIIGNMFD GIQRPLKKIN EISYGFIDEG IGLISIDEEK
     EWDVNIVVKV GDKLKPGDVY AEVQETNIIK HRIMVPQDVN GEVTKVKESG KYNIEEKIVT
     VKDGGNIYEL NLYQRWPVRT PRPIKNRLSL GKPLITGQRI LDMFFPIAKG GTVAIPGGFG
     TGKTMTQHQL AKWSDADIIV YIGCGERGNE MTEVLEDFPK LIDPKTNTSL MNRTVLIANT
     SNMPVAAREA SIYTGITIAE YYRDMGYDVA IMADSTSRWA EALREISGRL EEMPAEEGYP
     AYLPSRIAEF YERAGYVENL NDTEGSVTVI GAVSPAGADF SEPVTQNTKR FVGAFLGLDR
     KLAYARHYPA INWLTSYSQY NVMLTDWYLE NISEDIIELR NKMLKILFEE NKLQEIVKLV
     GEDVLPDDQR LILEVARILK VGFLQQNAYH DEDTYVPKEK QYKMLKAIEL FYDNAYKCVK
     MGIPISKIRN EEIFGDLIKM KYNIPNEDIS GIKVIEEKIS SYYEELIEQY RK