ID   VATA_CLOB1              Reviewed;         590 AA.
AC   A7FWQ7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 89.
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=CLB_2567;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS33811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000726; ABS33811.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_033047490.1; NC_009697.1.
DR   AlphaFoldDB; A7FWQ7; -.
DR   SMR; A7FWQ7; -.
DR   GeneID; 5187881; -.
DR   KEGG; cba:CLB_2567; -.
DR   HOGENOM; CLU_008162_3_1_9; -.
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; Translocase; Transport.
FT   CHAIN           1..590
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000322460"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   590 AA;  65396 MW;  AA4169458B4B18AA CRC64;
     MKTGRVLKIS GPLVVAEGME EANIYDVVKV GEKRLIGEII EMREDRASIQ VYEETAGLAP
     GDPVITTGEP LSVELGPGLI EAMFDGIQRP LNAIKAKAGD FITKGVEVHS LDRDKKWHFT
     PVKKVGDTVE AGDVIGIVQE TSIVEHKIMV PYGIKGTIET IEEGDFTVVD TVAKVKDKDK
     VSDLMMMQKW PVRRGRPYGR KLNPAQPMIT GQRVIDTFFP VTKGGTACVP GPFGSGKTVV
     QHQLAKWADA QIVVYIGCGE RGNEMTDVLN EFPELKDPKT GEPLMKRTVL IANTSNMPVA
     AREASIYTGI TIGEYFRDMG YSIALMADST SRWAEALREM SGRLEEMPGD EGYPAYLGSR
     AAEFYERAGN VVSIGSEERE GALTVIGAVS PPGGDLSEPV TQATLRIVKV FWGLDAQLAY
     RRHFPAINWL NSYSLYIEKI SPWMDENVAS DWTALRIKAM SLLQEEASLE EIVRLVGIDA
     LSEKDRLKLE VAKSLREDYL QQNAFHEVDT YASLGKQYKM LKLVLFFYDE AQRALNAGVY
     LKELLDLEVR DKIARAKYIS EENIENIDAI FNELSEVIDQ LISKGGIMNA