ID   VATA_CLOBB              Reviewed;         592 AA.
AC   B2TP91;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=CLL_A2861;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) 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; CP001056; ACD24834.1; -; Genomic_DNA.
DR   RefSeq; WP_012425560.1; NC_018648.1.
DR   AlphaFoldDB; B2TP91; -.
DR   SMR; B2TP91; -.
DR   PRIDE; B2TP91; -.
DR   EnsemblBacteria; ACD24834; ACD24834; CLL_A2861.
DR   KEGG; cbk:CLL_A2861; -.
DR   PATRIC; fig|935198.13.peg.2822; -.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000001195; 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; Translocase; Transport.
FT   CHAIN           1..592
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000115637"
FT   BINDING         232..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   592 AA;  65064 MW;  619BF217AD95916D CRC64;
     MKTGKIIKVS GPLVVAEGMD EANIYDVCKV GEKGLIGEII EMRGDKASIQ VYEETSGIGP
     GDPVVTTGEP LSVELGPGLI ESMFDGIQRP LDAFMEAAKS SFLTRGVSVP SLNREKKWDF
     KPTAKVGDDV KSGTVIGTVQ ETPVVEQRIM IPIGIEGKIK EIKAGSFTVT ETIAIVETEK
     GDREVQLMQK WPVRKGRPYS AKINPVEPML TGQRVIDTFF PVAKGGAAAI PGPFGAGKTV
     TQHQIAKWGD AEIVVYVGCG ERGNEMTDVV NEFPELIDPK TGESLMKRTV LIANTSNMPV
     AAREASIYTG ITIAEYFRDM GYSVSIMADS TSRWAEALRE MSGRLEEMPG DEGYPAYLGS
     RLADYYERAG KVECLGNDGR IGSITAIGAV SPPGGDISEP VSQSTLRIVK VFWGLDAQLA
     YQRHFPTINW LTSYSLYADT IDKWMNGNVA ENWGALRLEA MTILQDEAQL QEIVRLVGID
     ALSEKDRLKL DVAKSIREDY LQQNGFHEID TYTSLKKQYK MLNLILGYRK EAERALEAGV
     YLNDILAMED LKDRIARSKY IHEDDLEKMD QIVVDLKNAI DNLINKGGVA NA