| IED ID | IndEnz0002014373 |
| Enzyme Type ID | protease014373 |
| Protein Name |
Cysteine protease avirulence protein AvrRpt2 Avirulence protein AvrRpt2 EC 3.4.22.- |
| Gene Name | avrRpt2 |
| Organism | Pseudomonas syringae pv. tomato |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas syringae group Pseudomonas syringae group genomosp. 3 Pseudomonas syringae pv. tomato |
| Enzyme Sequence | MKIAPVAINHSPLSREVPSHAAPTQAKQTNLQSEAGDLDARKSSASSPETRALLATKTVLGRHKIEVPAFGGWFKKKSSKHETGGSSANADSSSVASDSTEKPLFRLTHVPYVSQGNERMGCWYACARMVGHSVEAGPRLGLPELYEGREGPAGLQDFSDVERFIHNEGLTRVDLPDNERFTHEELGALLYKHGPIIFGWKTPNDSWHMSVLTGVDKETSSITFHDPRQGPDLAMPLDYFNQRLAWQVPHAMLYR |
| Enzyme Length | 255 |
| Uniprot Accession Number | Q6LAD6 |
| Absorption | |
| Active Site | ACT_SITE 122; /note=Nucleophile; ACT_SITE 208; ACT_SITE 226 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Effector protein involved in gene-for-gene resistance in plants expressing RPS2. Its thiol protease activity is required for the degradation of plant cell RIN4 and consequent activation of RPS2 during bacterial infection. The activation of RPS2 is sufficient for the induction of hypersensitive response (HR) and plant resistance. Cleavage of RIN4 by AvrRpt2 also interferes with RPM1-mediated resistance activated by either AvrRpm1 or AvrB. Contributes to virulence in plants lacking the resistance protein RPS2 promoting pathogen growth and disease symptoms. Inhibits PAMP (pathogen-associated molecular patterns)-induced signaling compromising the host's basal defense system. Blocks plant callose deposition, flg22 (a peptide corresponding to the most conserved domain of flagellin) induced accumulation of PR-1, PR-2 and PR-5 and activation of GST6 transcription. The mechanism of virulence is unknown, but this activity is independent of ethylene and salicylic acid response pathways and independent of RIN4 disappearance. {ECO:0000269|PubMed:11106023, ECO:0000269|PubMed:12950919, ECO:0000269|PubMed:15000398, ECO:0000269|PubMed:15746386, ECO:0000269|PubMed:16042008}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Erroneous initiation (1); Mutagenesis (22); Propeptide (1); Region (3); Sequence conflict (2); Site (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Host cell membrane;Host membrane;Hydrolase;Hypersensitive response elicitation;Membrane;Protease;Secreted;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10361296, ECO:0000269|PubMed:11204781, ECO:0000269|PubMed:14526114}. Host cell membrane {ECO:0000269|PubMed:14526114}. Note=Secreted via type III secretion system (TTSS) (PubMed:14526114). Localized to the plant cell membrane (PubMed:14526114). |
| Modified Residue | |
| Post Translational Modification | PTM: Autocleaved inside plant cells upon activation by cyclophilin. Cleavage is crucial in subcellular location and in eliciting HR. Inhibited by cyclosporin A (cyclophilin inhibitor). |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,158 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |