A8GG79 · TRI1_SERP5
- ProteinADP-ribosylarginine hydrolase Tri1
- Genetri1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids366 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Immunity component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts as an arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. De-ADP-ribosylates FtsZ, is able to act on other proteins as well. Neutralizes the toxic activity of cognate toxin Tre1-Sp. Expression of this protein alone in E.coli partially protects the cells against competition by wild-type S.proteamaculans. Neutralizes Tre1-Sp both by occluding its active site via its N-terminal extension and by hydrolyzing the ADP-ribosyl moiety from FtsZ; the 2 activities are dissociable by mutagenesis.
Catalytic activity
- N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + H2O = ADP-D-ribose + L-arginyl-[protein]
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ADP-ribosylarginine hydrolase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-ribosylarginine hydrolase Tri1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionA8GG79
Phenotypes & Variants
Disruption phenotype
A double tre1-tri1 deletion is outcompeted by wild-type cells, but not by wild-type cells missing a type 6 secretion system (T6SS).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 32 | Partially protects E.coli against cognate toxin Tre1. No longer protects E.coli; when associated with N-161. | ||||
Sequence: R → E | ||||||
Mutagenesis | 161 | Partially protects E.coli against cognate toxin Tre1, no longer de-ADP-ribosylates FtsZ. No longer protects E.coli; when associated with E-32. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446517 | 1-366 | ADP-ribosylarginine hydrolase Tri1 | |||
Sequence: MIDLREDTWTLQLYAQRYKGLSPKNSRELQLRMEYDPLKPNLPTSGEEQNSKPEWLNTPPCLIPESESLDKAKGALVGLAIGDAIGTTLEFLPRDKLHVNDMVGGGPFRLQPGEWTDDTSMALCLAESYISAGRLDITLFREKLVRWYRHGENSSNGRCFDIGNTTRNALEQYLKHGASWFGNTEPETAGNAAIIRQAPTSIFRRKSLQRTFADSDSQSMATHCAPESMASCQFLGFILNYLINGSSREKAFSPHVMPLPVRVLLINAGEYKEKKRDEIRSSGYVIDTLEAAMWAVWNTDNFHDAILLAANLGDDADSVAATTGQIAGALYGYSNIPKPWLDKLVQQERISNLAEQLFYMAPEEDF |
Interaction
Subunit
Forms a stable complex with cognate effector protein Tre1-Sp.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-65 | N-terminal extension | ||||
Sequence: MIDLREDTWTLQLYAQRYKGLSPKNSRELQLRMEYDPLKPNLPTSGEEQNSKPEWLNTPPCLIPE | ||||||
Region | 74-366 | ADP-ribosyl hydrolase domain | ||||
Sequence: GALVGLAIGDAIGTTLEFLPRDKLHVNDMVGGGPFRLQPGEWTDDTSMALCLAESYISAGRLDITLFREKLVRWYRHGENSSNGRCFDIGNTTRNALEQYLKHGASWFGNTEPETAGNAAIIRQAPTSIFRRKSLQRTFADSDSQSMATHCAPESMASCQFLGFILNYLINGSSREKAFSPHVMPLPVRVLLINAGEYKEKKRDEIRSSGYVIDTLEAAMWAVWNTDNFHDAILLAANLGDDADSVAATTGQIAGALYGYSNIPKPWLDKLVQQERISNLAEQLFYMAPEEDF |
Domain
The N-terminal extension forms a projection that reaches into the active site of cognate toxin Tre1-Sp where it occludes the active site.
Sequence similarities
Belongs to the ADP-ribosylglycohydrolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length366
- Mass (Da)40,934
- Last updated2007-11-13 v1
- ChecksumA9443B5B3280CC54
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000826 EMBL· GenBank· DDBJ | ABV42119.1 EMBL· GenBank· DDBJ | Genomic DNA |