DARG_MYCBP
ID DARG_MYCBP Reviewed; 352 AA.
AC A0A0H3M776;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=DNA ADP-ribosyl glycohydrolase {ECO:0000303|PubMed:34408320};
DE Short=DarG {ECO:0000303|PubMed:34408320};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:O53605};
DE AltName: Full=Antitoxin DarG {ECO:0000303|PubMed:34408320};
GN Name=darG {ECO:0000303|PubMed:34408320};
GN OrderedLocusNames=BCG_0091 {ECO:0000312|EMBL:CAL70075.1};
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:CAL70075.1}
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 FUNCTION AS AN ANTITOXIN, INDUCTION BY DNA DAMAGE, AND DISRUPTION
RP PHENOTYPE.
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: Antitoxin component of a hybrid type II/IV toxin-antitoxin
CC (TA) system. De-ADP-ribosylates DNA (probably) modified on thymidine by
CC its cognate toxin DarT, which neutralizes the activity of cognate toxin
CC DarT. {ECO:0000250|UniProtKB:O53605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(ADP-alpha-D-ribosyl)-thymidine in DNA + H2O = a
CC thymidine in DNA + ADP-D-ribose; Xref=Rhea:RHEA:71655, Rhea:RHEA-
CC COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:137386, ChEBI:CHEBI:191199;
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71656;
CC Evidence={ECO:0000250|UniProtKB:O53605};
CC -!- SUBUNIT: Forms a complex with cognate toxin DarT; this complex
CC neutralizes the toxic effect of DarT. {ECO:0000250|UniProtKB:O53605}.
CC -!- INDUCTION: By DNA damage (mitomycin C) as well as by darT
CC overexpression. {ECO:0000269|PubMed:34408320}.
CC -!- DISRUPTION PHENOTYPE: Knock-down of darG expression leads to increased
CC ADP-ribosylation of genomic DNA by DarT and induction of the DNA damage
CC response including recA, dnaB and dnaE2; darT and darG are also
CC induced. {ECO:0000269|PubMed:34408320}.
CC -!- SIMILARITY: Belongs to the DarG ADP-ribosyl glycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; AM408590; CAL70075.1; -; Genomic_DNA.
DR RefSeq; WP_003400551.1; NC_008769.1.
DR SMR; A0A0H3M776; -.
DR GeneID; 45424019; -.
DR KEGG; mbb:BCG_0091; -.
DR HOGENOM; CLU_049707_0_0_11; -.
DR OMA; WIVNFPT; -.
DR Proteomes; UP000001472; Chromosome.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Toxin-antitoxin system.
FT CHAIN 1..352
FT /note="DNA ADP-ribosyl glycohydrolase"
FT /id="PRO_0000456045"
FT DOMAIN 1..155
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
FT BINDING 8..9
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
FT BINDING 20..22
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
FT BINDING 31..34
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
FT BINDING 79
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
FT BINDING 117..121
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0000250|UniProtKB:P0DV57"
SQ SEQUENCE 352 AA; 38563 MW; CE3CA7024B953593 CRC64;
MITYGSGDLL RADTEALVNT VNCVGVMGKG IALQFKRRYP EMFTAYEKAC KRGEVTIGKM
FVVDTGQLDG PKHIINFPTK KHWRAPSKLA YIDAGLIDLI RVIRELNIAS VAVPPLGVGN
GGLDWEDVEQ RLVSAFQQLP DVDAVIYPPS GGSRAIEGVE GLRMTWGRAV ILEAMRRYLQ
QRRAMEPWED PAGISHLEIQ KLMYFANEAD PDLALDFTPG RYGPYSERVR HLLQGMEGAF
TVGLGDGTAR VLANQPISLT TKGTDAITDY LATDAAADRV SAAVDTVLRV IEGFEGPYGV
ELLASTHWVA TREGAKEPAT AAAAVRKWTK RKGRIYSDDR IGVALDRILM TA
