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DART_MYCBP
ID   DART_MYCBP              Reviewed;         230 AA.
AC   A0A0H3M0L1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=DNA ADP-ribosyl transferase {ECO:0000303|PubMed:34408320};
DE            Short=DarT {ECO:0000303|PubMed:34408320};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:O53604};
DE   AltName: Full=Toxin DarT {ECO:0000303|PubMed:34408320};
GN   Name=darT {ECO:0000303|PubMed:34408320};
GN   OrderedLocusNames=BCG_0090 {ECO:0000312|EMBL:CAL70074.1};
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1] {ECO:0000312|EMBL:CAL70074.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [2]
RP   INDUCTION BY DNA DAMAGE.
RC   STRAIN=BCG;
RX   PubMed=34408320; DOI=10.1038/s41586-021-03825-4;
RA   Schuller M., Butler R.E., Ariza A., Tromans-Coia C., Jankevicius G.,
RA   Claridge T.D.W., Kendall S.L., Goh S., Stewart G.R., Ahel I.;
RT   "Molecular basis for DarT ADP-ribosylation of a DNA base.";
RL   Nature 596:597-602(2021).
CC   -!- FUNCTION: Toxic component of a hybrid type II/IV toxin-antitoxin (TA)
CC       system. ADP-ribosylates ssDNA, preferentially in the motif TTTW. Its
CC       toxic effect is neutralized by cognate antitoxin DarG.
CC       {ECO:0000250|UniProtKB:O53604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a thymidine in DNA + NAD(+) = an N-(ADP-alpha-D-ribosyl)-
CC         thymidine in DNA + H(+) + nicotinamide; Xref=Rhea:RHEA:71651,
CC         Rhea:RHEA-COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:137386,
CC         ChEBI:CHEBI:191199;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71652;
CC         Evidence={ECO:0000250|UniProtKB:O53604};
CC   -!- SUBUNIT: Forms a complex with cognate antitoxin DarG; this complex
CC       neutralizes the toxic effect of DarT. {ECO:0000250|UniProtKB:O53604}.
CC   -!- INDUCTION: By DNA damage (mitomycin C) as well as by darT
CC       overexpression. {ECO:0000269|PubMed:34408320}.
CC   -!- DOMAIN: The NAD(+)-binding element stabilizes the ADP-ribosylating
CC       turn-turn (ARTT) loop which confers substrate specificity; both domains
CC       contribute to ssDNA-binding. {ECO:0000250|UniProtKB:A0A0B0SG80}.
CC   -!- SIMILARITY: Belongs to the DarT ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AM408590; CAL70074.1; -; Genomic_DNA.
DR   RefSeq; WP_003400548.1; NC_008769.1.
DR   SMR; A0A0H3M0L1; -.
DR   GeneID; 45424018; -.
DR   KEGG; mbb:BCG_0090; -.
DR   HOGENOM; CLU_113641_1_0_11; -.
DR   OMA; HDYVPFY; -.
DR   Proteomes; UP000001472; Chromosome.
DR   InterPro; IPR029494; DarT.
DR   Pfam; PF14487; DarT; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Glycosyltransferase; Nucleotidyltransferase;
KW   Toxin-antitoxin system; Transferase.
FT   CHAIN           1..230
FT                   /note="DNA ADP-ribosyl transferase"
FT                   /id="PRO_0000456049"
FT   DOMAIN          29..230
FT                   /note="DarT"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT   BINDING         30..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT   BINDING         67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
SQ   SEQUENCE   230 AA;  25580 MW;  1A109D34B16590A8 CRC64;
     MITRYKPESG FVARSGGPDR KRPHDWIVWH FTHADNLPGI ITAGRLLADS AVTPTTEVAY
     NPVKELRRHK VVAPDSRYPA SMASDHVPFY IAARSPMLYV VCKGHSGYSG GAGPLVHLGV
     ALGDIIDADL TWCASDGNAA ASYTKFSRQV DTLGTFVDFD LLCQRQWHNT DDDPNRQSRR
     AAEILVYGHV PFELVSYVCC YNTETMTRVR TLLDPVGGVR KYVIKPGMYY
 
 
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