DARTG_THEA7
ID DARTG_THEA7 Reviewed; 388 AA.
AC K2PFJ6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=DNA ADP-ribosyl transferase-DNA ADP-ribosyl glycohydrolase fusion protein {ECO:0000305};
DE Short=DarTG {ECO:0000303|PubMed:34408320};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:O53604};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:O53605};
GN Name=darTG {ECO:0000305};
GN ORFNames=H17ap60334_07413 {ECO:0000312|EMBL:EKF49129.1};
OS Thermosipho africanus (strain H17ap60334).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=1161912;
RN [1] {ECO:0000312|EMBL:EKF49129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H17ap60334 {ECO:0000312|EMBL:EKF49129.1};
RA Nesbo C.L., Swithers K., Dlutek M., Marquis P., Doolittle F.W.;
RT "Genome sequence of Thermosipho africanus H17ap60334.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:7OMU}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) IN COMPLEX WITH ADP-RIBOSE.
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: A fusion protein of the toxic and antitoxin components of a
CC hybrid type II/IV toxin-antitoxin (TA) system. The N-terminal domain
CC ADP-ribosylates ssDNA on a thymidine residue, while the C-terminal
CC domain removes the modification, neutralizing the toxic effect.
CC {ECO:0000250|UniProtKB:O53604, ECO:0000250|UniProtKB:O53605}.
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 -!- 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 -!- 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: In the N-terminal section; belongs to the DarT ADP-
CC ribosyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DarG ADP-ribosyl
CC glycohydrolase family. {ECO:0000305}.
CC -!- CAUTION: This is a fusion of 2 opposing activites; its in vivo function
CC is unclear. {ECO:0000305}.
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DR EMBL; AJIP01000032; EKF49129.1; -; Genomic_DNA.
DR RefSeq; WP_004103096.1; NZ_AJIP01000032.1.
DR PDB; 7OMU; X-ray; 2.96 A; AAA/BBB=1-388.
DR PDBsum; 7OMU; -.
DR SMR; K2PFJ6; -.
DR EnsemblBacteria; EKF49129; EKF49129; H17ap60334_07413.
DR PATRIC; fig|1161912.4.peg.1460; -.
DR Proteomes; UP000007132; Unassembled WGS sequence.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR029494; DarT.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF14487; DarT; 1.
DR Pfam; PF01661; Macro; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Glycosyltransferase; Hydrolase;
KW Nucleotidyltransferase; Toxin-antitoxin system; Transferase.
FT CHAIN 1..388
FT /note="DNA ADP-ribosyl transferase-DNA ADP-ribosyl
FT glycohydrolase fusion protein"
FT /id="PRO_0000456053"
FT DOMAIN 9..196
FT /note="DarT"
FT /evidence="ECO:0000255"
FT DOMAIN 196..376
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 34..52
FT /note="NAD(+)-binding element"
FT /evidence="ECO:0000269|PubMed:34408320"
FT REGION 107..152
FT /note="ADP-ribosylating turn-turn loop"
FT /evidence="ECO:0000269|PubMed:34408320"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT ACT_SITE 152
FT /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT BINDING 10..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT BINDING 50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0SG80"
FT BINDING 215..216
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0007744|PDB:7OMU"
FT BINDING 227..229
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0007744|PDB:7OMU"
FT BINDING 301
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0007744|PDB:7OMU"
FT BINDING 339..343
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0007744|PDB:7OMU"
FT BINDING 371..372
FT /ligand="ADP-D-ribose"
FT /ligand_id="ChEBI:CHEBI:57967"
FT /evidence="ECO:0007744|PDB:7OMU"
SQ SEQUENCE 388 AA; 44883 MW; AB552526040312B8 CRC64;
MFPRFRELYY ITHIDNVPSI LEKGILSHAE IERQSINCKK VYDNSIVLKR KSRLLADNRS
LWEFANLYFQ PRNPMLYRLL VQGLKPKDLA IVAVKWTIMK RDDILITDGN AASSETQIYR
KSEIKNIKNI ISVKDMEYWR EEDGSKRKIM AECLVPQCVD PRYISAIYVS DHEVASNLKK
AINNRNIPVI PDPTFFFLPN REIKLTQNLS LVEGDMFFSR MQTLTVSVNT VGVMGKGLAS
RVKYQFPDVY VVFQDACKKK ELEFGKPYLY KRESSLDAFL AEDGEKLSDL NHQTWFLLFP
TKRHWKNMSE IKGIESGLRW IVENYKKEGI KSLAVPALGC GLGGLEWSIV GPLMCRYLTK
LEIPVQIYLP LEKRIPDVQL SPKFLLDS
