TRI1_PSEPG
ID TRI1_PSEPG Reviewed; 371 AA.
AC B0KTG8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=ADP-ribosylarginine hydrolase Tri1 {ECO:0000305};
DE EC=3.2.2.19 {ECO:0000305|PubMed:30343895};
DE AltName: Full=Immunity protein Tri1 {ECO:0000303|PubMed:30343895};
DE Short=Tri1-Pp {ECO:0000303|PubMed:30343895};
GN Name=tri1 {ECO:0000303|PubMed:30343895}; OrderedLocusNames=PputGB1_2761;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF ASP-157.
RC STRAIN=GB-1;
RX PubMed=30343895; DOI=10.1016/j.cell.2018.09.037;
RA Ting S.Y., Bosch D.E., Mangiameli S.M., Radey M.C., Huang S., Park Y.J.,
RA Kelly K.A., Filip S.K., Goo Y.A., Eng J.K., Allaire M., Veesler D.,
RA Wiggins P.A., Peterson S.B., Mougous J.D.;
RT "Bifunctional immunity proteins protect bacteria against FtsZ-targeting
RT ADP-ribosylating toxins.";
RL Cell 175:1380-1392(2018).
CC -!- FUNCTION: Immunity component of an interbacterial competition system
CC (also called effector-immunity systems). Expression in E.coli
CC neutralizes the toxic effects of non-cognate S.proteamaculans effector
CC protein Tre1 (Tre1-Sp); cannot be co-purified with Tre1-Sp from E.coli,
CC suggesting they do not form a stable complex (PubMed:30343895).
CC Probably acts as an arginine mono-ADP-ribosylhydrolase, mediating the
CC removal of mono-ADP-ribose attached to arginine residues on proteins.
CC Probably de-ADP-ribosylates FtsZ and possibly other proteins; the
CC ability to hydrolyze ADP-ribosyl moieties is not essential for
CC neutralization of its cognate toxin, strongly suggesting its N-terminal
CC extension occludes the active site of cognate toxin Tre1 (Probable).
CC {ECO:0000269|PubMed:30343895, ECO:0000305|PubMed:30343895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-
CC ribose + L-arginyl-[protein]; Xref=Rhea:RHEA:14885, Rhea:RHEA-
CC COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29965, ChEBI:CHEBI:57967, ChEBI:CHEBI:142554;
CC EC=3.2.2.19; Evidence={ECO:0000305|PubMed:30343895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A8GG79};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:A8GG79};
CC -!- DOMAIN: The N-terminal extension probably forms a projection that
CC reaches into the active site of cognate toxin Tre1-Pp where it occludes
CC the active site. {ECO:0000305|PubMed:30343895}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; CP000926; ABY98655.1; -; Genomic_DNA.
DR RefSeq; WP_012272394.1; NC_010322.1.
DR AlphaFoldDB; B0KTG8; -.
DR SMR; B0KTG8; -.
DR STRING; 76869.PputGB1_2761; -.
DR EnsemblBacteria; ABY98655; ABY98655; PputGB1_2761.
DR KEGG; ppg:PputGB1_2761; -.
DR eggNOG; COG1397; Bacteria.
DR HOGENOM; CLU_024566_8_4_6; -.
DR OMA; PGTWTDD; -.
DR Proteomes; UP000002157; Chromosome.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..371
FT /note="ADP-ribosylarginine hydrolase Tri1"
FT /id="PRO_0000446518"
FT REGION 1..61
FT /note="N-terminal extension"
FT /evidence="ECO:0000305|PubMed:30343895"
FT REGION 70..362
FT /note="ADP-ribosyl hydrolase domain"
FT /evidence="ECO:0000305|PubMed:30343895"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT MUTAGEN 157
FT /note="D->N: No longer protects E.coli against
FT S.proteamaculans effector protein Tre1, no effect on growth
FT in the absence of S.proteamaculans."
FT /evidence="ECO:0000269|PubMed:30343895"
SQ SEQUENCE 371 AA; 40782 MW; C4452DAF28CD5029 CRC64;
MIDLRSPNAL LSDYVERYAH LSPEPSRQLQ QRMDYNVRAD APAEPASKPR WLQSRACTLT
PEQALDRAKG ALLGLAIGDA VGTTLEFLPR DREHVNDMVG GGPFRLAAGE WTDDTSMALC
LADTYVSQGK FDYATYANAL VRWYRHGENS VNGRCFDIGN ATRNALEGWL REGIGWQGNY
DPSTAGNGSI IRLAPTAIFR RHSLSASWWE SVTQSSVTHN ADEAVNCCQL LAAQLHLALN
GADKEETLAP AVRSLRPRPM IINAGEYKQK SRDQIRSSGY VVDTLEAALW AVWNSNNFHD
AILLAANLAD DADSVAATAG QLAGALYGVS GMPPEWVEKV AWSQHIQKLA QELFDRAPQV
DELDALLYGK R
