VATA_CLOBH
ID VATA_CLOBH Reviewed; 590 AA.
AC A5I557; A7G6C3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=CBO2625, CLC_2498;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / 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=ABS38064.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAL84184.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000727; ABS38064.1; ALT_INIT; Genomic_DNA.
DR EMBL; AM412317; CAL84184.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_033047490.1; NC_009698.1.
DR RefSeq; YP_001255122.1; NC_009495.1.
DR RefSeq; YP_001388338.1; NC_009698.1.
DR AlphaFoldDB; A5I557; -.
DR SMR; A5I557; -.
DR PRIDE; A5I557; -.
DR GeneID; 5187881; -.
DR KEGG; cbh:CLC_2498; -.
DR KEGG; cbo:CBO2625; -.
DR PATRIC; fig|413999.7.peg.2607; -.
DR HOGENOM; CLU_008162_3_1_9; -.
DR PRO; PR:A5I557; -.
DR Proteomes; UP000001986; 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; IBA:GO_Central.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
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..590
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000322461"
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
