VATA_CLOBL
ID VATA_CLOBL Reviewed; 590 AA.
AC A7GGL4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=CLI_2690;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS41807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000728; ABS41807.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041173237.1; NC_009699.1.
DR AlphaFoldDB; A7GGL4; -.
DR SMR; A7GGL4; -.
DR EnsemblBacteria; ABS41807; ABS41807; CLI_2690.
DR KEGG; cbf:CLI_2690; -.
DR HOGENOM; CLU_008162_3_1_9; -.
DR Proteomes; UP000002410; 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; Translocase; Transport.
FT CHAIN 1..590
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000322462"
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; 65540 MW; 736A6829ECDCF7F8 CRC64;
MKTGRVLKIS GPLVVAEGME EANIYDVVKV GEKRLIGEII EMREDRASIQ VYEETAGLAP
GDPVITTGEP LSVELGPGLI EAMFDGIQRP LNAIKAKAGD FITRGVEVHS LDRDRKWHFT
PVKKVGDTVE AGDVIGIVQE TSIVEHKIMV PYGIKGTIET IEEGDFTVVD TVAKVKDKDK
VSDLIMMQKW PVRRGRPYGR KLNPVEPMIT GQRVIDTFFP VTKGGTACVP GPFGSGKTVV
QHQLAKWADA QIVVYIGCGE RGNEMTDVLN EFPELKDPKT GEPLMKRTVL IANTSNMPVA
AREASIYTGI TIGEYFRDMG YSVALMADST SRWAEALREM SGRLEEMPGD EGYPAYLGSR
AADFYERAGK VLSLGSEGRE GALTVIGAVS PPGGDLSEPV TQATLRIVKV FWGLDSQLAY
RRHFPAINWL NSYSLYLEKI SPWMDENVAS DWTALRTRAM SLLQEEANLE EIVRLVGIDA
LSEKDRLKLE VAKSLREDYL QQNAFHEVDT YASLEKQYKM LKLVLFFYDE TQRALNAGIY
LKELLDLEVR DKIARAKYIS EESIENIDAI FNELSEVIDE LISKGGIMNA