TRI1_PSEP8
ID TRI1_PSEP8 Reviewed; 382 AA.
AC A0A168WVR6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
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};
GN Name=tri1 {ECO:0000303|PubMed:30343895}; ORFNames=KKK_13285;
OS Pseudomonas putida (strain DSM 28064 / B6-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1081940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28064 / B6-2;
RX PubMed=22072645; DOI=10.1128/jb.06201-11;
RA Tang H., Yu H., Li Q., Wang X., Gai Z., Yin G., Su F., Tao F., Ma C.,
RA Xu P.;
RT "Genome sequence of Pseudomonas putida strain B6-2, a superdegrader of
RT polycyclic aromatic hydrocarbons and dioxin-like compounds.";
RL J. Bacteriol. 193:6789-6790(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 28064 / B6-2;
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: Orphan immunity component of an interbacterial competition
CC system (also called effector-immunity systems); this bacteria does not
CC encode an identifiable cognate effector protein. Expression of this
CC protein in E.coli partially protects the cells against competition by
CC wild-type S.proteamaculans (PubMed:30343895). Probably acts as an
CC arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-
CC ribose attached to arginine residues on proteins. Probably de-ADP-
CC ribosylates FtsZ and possibly other proteins (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:0000250|UniProtKB:A8GG79};
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 -!- DISRUPTION PHENOTYPE: Decreased fitness in interbacterial competition
CC assays against S.proteamaculans. {ECO:0000269|PubMed:30343895}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; CP015202; ANC81935.1; -; Genomic_DNA.
DR RefSeq; WP_019751692.1; NZ_CP015202.1.
DR AlphaFoldDB; A0A168WVR6; -.
DR SMR; A0A168WVR6; -.
DR EnsemblBacteria; ANC81935; ANC81935; KKK_13285.
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 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..382
FT /note="ADP-ribosylarginine hydrolase Tri1"
FT /id="PRO_0000446519"
FT REGION 12..72
FT /note="N-terminal extension"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT REGION 81..373
FT /note="ADP-ribosyl hydrolase domain"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8GG79"
SQ SEQUENCE 382 AA; 41685 MW; 8325E239C88FA537 CRC64;
MDESNLLQGI SMIDLRSPDA ILSDYAKRYA HLLPELSPQL QQRMAYMPEP DAPRLPLTKP
AWLSDRSCTL TPGQAIDRAQ GALLGLAIGD AVGTTLEFRR RDQGQVSDMV GGGPFRLAPG
EWTDDTSMAL CLADTYASQG KFDFATFADA MVRWYRQGEN SANGRCFDIG NVTRRALEGW
EAQGLAWMGN LEASTAGNGS LIRLAPTAIF RRHSLSATWW ESVTQSSVTH RAIEVSECCK
LFGAQLHLAL NGADKEEALS PKVRPLQPRA LIINAGEYKH KTREQIRSSG YVVDTLEAAL
WAVWNTDNFR DAILLAANLA DDADSVAATA GQIAGALYGV SGMPPEWVAK VAWSRHICEL
ASRLFELAPQ GDEMDELLSG SE
