DART_THES0
ID DART_THES0 Reviewed; 209 AA.
AC A0A0B0SG80;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=DNA ADP-ribosyl transferase {ECO:0000303|PubMed:34408320};
DE Short=DarT {ECO:0000303|PubMed:34408320};
DE EC=2.4.2.- {ECO:0000269|PubMed:34408320};
DE AltName: Full=Toxin DarT {ECO:0000303|PubMed:34408320};
GN Name=darT {ECO:0000303|PubMed:34408320};
GN ORFNames=QT17_01930 {ECO:0000312|EMBL:KHG66095.1};
OS Thermus sp. (strain 2.9).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus;
OC unclassified Thermus.
OX NCBI_TaxID=1577051;
RN [1] {ECO:0000312|EMBL:KHG66095.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2.9 {ECO:0000312|EMBL:KHG66095.1};
RX PubMed=25593256; DOI=10.1128/genomea.01414-14;
RA Navas L.E., Berretta M.F., Ortiz E.M., Benintende G.B., Amadio A.F.,
RA Zandomeni R.O.;
RT "Draft Genome Sequence of Thermus sp. Isolate 2.9, Obtained from a Hot
RT Water Spring Located in Salta, Argentina.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0007744|PDB:7OMV, ECO:0007744|PDB:7OMW, ECO:0007744|PDB:7OMX}
RP X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) ALONE AND IN COMPLEX WITH NAD+ WITH
RP AND WITHOUT DNA, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP POSSIBLE REACTION MECHANISM, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ARG-154
RP AND GLU-160, AND DNA-BINDING.
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 on the second thymidine of the consensus
CC sequence 5'-TNTC-3'; the protein does not auto-modify. Arg-51 is highly
CC flexible, allowing it to assume multiple positions in the crystal
CC structures (PubMed:34408320). Its toxic effect is neutralized by
CC cognate antitoxin DarG (By similarity). {ECO:0000250|UniProtKB:O53604,
CC ECO:0000269|PubMed:34408320}.
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:0000269|PubMed:34408320};
CC -!- SUBUNIT: Probably forms a complex with cognate antitoxin DarG; this
CC complex might decrease ADP-ribosylation activity of DarT.
CC {ECO:0000250|UniProtKB:P0DV56}.
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:0000269|PubMed:34408320}.
CC -!- SIMILARITY: Belongs to the DarT ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; JTJB01000003; KHG66095.1; -; Genomic_DNA.
DR RefSeq; WP_039455677.1; NZ_JTJB01000003.1.
DR PDB; 7OMV; X-ray; 1.29 A; AAA=1-209.
DR PDB; 7OMW; X-ray; 1.30 A; AAA=1-209.
DR PDB; 7OMX; X-ray; 1.52 A; AAA=1-209.
DR PDB; 7OMY; X-ray; 1.60 A; AAA=1-209.
DR PDB; 7OMZ; X-ray; 1.66 A; AAA=1-209.
DR PDB; 7ON0; X-ray; 1.46 A; AAA=1-209.
DR PDBsum; 7OMV; -.
DR PDBsum; 7OMW; -.
DR PDBsum; 7OMX; -.
DR PDBsum; 7OMY; -.
DR PDBsum; 7OMZ; -.
DR PDBsum; 7ON0; -.
DR SMR; A0A0B0SG80; -.
DR STRING; 1577051.QT17_01930; -.
DR EnsemblBacteria; KHG66095; KHG66095; QT17_01930.
DR Proteomes; UP000030683; Unassembled WGS sequence.
DR InterPro; IPR029494; DarT.
DR Pfam; PF14487; DarT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Glycosyltransferase; Nucleotidyltransferase;
KW Toxin-antitoxin system; Transferase.
FT CHAIN 1..209
FT /note="DNA ADP-ribosyl transferase"
FT /id="PRO_0000456052"
FT DOMAIN 12..209
FT /note="DarT"
FT /evidence="ECO:0000255"
FT DNA_BIND 44..50
FT /evidence="ECO:0000269|PubMed:34408320,
FT ECO:0007744|PDB:7OMY"
FT DNA_BIND 75..80
FT /evidence="ECO:0000269|PubMed:34408320,
FT ECO:0007744|PDB:7OMY"
FT DNA_BIND 145..148
FT /evidence="ECO:0000269|PubMed:34408320,
FT ECO:0007744|PDB:7OMY"
FT DNA_BIND 154..158
FT /evidence="ECO:0000269|PubMed:34408320,
FT ECO:0007744|PDB:7OMY"
FT REGION 35..53
FT /note="NAD(+)-binding element"
FT /evidence="ECO:0000269|PubMed:34408320"
FT REGION 116..160
FT /note="ADP-ribosylating turn-turn loop"
FT /evidence="ECO:0000269|PubMed:34408320"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:34408320"
FT ACT_SITE 160
FT /evidence="ECO:0000305|PubMed:34408320,
FT ECO:0007744|PDB:7OMY"
FT BINDING 13..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:7OMW"
FT BINDING 22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:7OMW"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:7OMW"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:7OMW"
FT SITE 154
FT /note="Specifically recognizes first thymidine of consensus
FT sequence 5'-TGTC-3'"
FT /evidence="ECO:0000269|PubMed:34408320"
FT MUTAGEN 154
FT /note="R->W: No longer toxic in vivo, no longer ADP-
FT ribosylates ssDNA."
FT /evidence="ECO:0000269|PubMed:34408320"
FT MUTAGEN 160
FT /note="E->A: Nearly completely loss of DNA ADP-
FT ribosylation."
FT /evidence="ECO:0000269|PubMed:34408320"
SQ SEQUENCE 209 AA; 24371 MW; 6B05FEDE9FC2A0D8 CRC64;
MKRTYPEPTP IYHITHIDNL KGILRMGKLL AHNQSPPKQR SIAYAHIQER RNRAKVPQPP
GGVLHDYVPF YFCPRSPMLY AIYSGATEYQ GGQEPILHLV SSAQAVHKAG LPFVFTDRHG
VLSHARFFRQ LEELAQLDWE AIQASYWADP PELREKKQAE FLVYKAFPWA LIEEIAVYSQ
RVGEEVLKIL KQFPEARRPR VCIRKDWYY
