IED ID | IndEnz0002005136 |
Enzyme Type ID | protease005136 |
Protein Name |
Cysteine protease avirulence protein AvrPphB EC 3.4.22.- Cleaved into: 7 kDa product; 28 kDa product |
Gene Name | avrPph3 |
Organism | Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas syringae group Pseudomonas syringae group genomosp. 2 Pseudomonas savastanoi (Pseudomonas syringae pv. savastanoi) Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola) |
Enzyme Sequence | MKIGTQATSLAVLHNQESHAPQAPIAVRPEPAHAIPEIPLDLAIRPRTRGIHPFLAMTLGDKGCASSSGVSLEDDSHTQVSLSDFSVASRDVNHNNICAGLSTEWLVMSSDGDAESRMDHLDYNGEGQSRGSERHQVYNDALRAALSNDDEAPFFTASTAVIEDAGFSLRREPKTVHASGGSAQLGQTVAHDVAQSGRKHLLSLRFANVQGHAIACSCEGSQFKLFDPNLGEFQSSRSAAPQLIKGLIDHYNSLNYDVACVNEFRVS |
Enzyme Length | 267 |
Uniprot Accession Number | Q52430 |
Absorption | |
Active Site | ACT_SITE 98; ACT_SITE 212; ACT_SITE 227 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease avirulence protein, which is essential during infection of plant cells from cultivar-specific of beans and Arabidopsis thaliana. The autocleavage of the protein is required for virulence function. May act by affecting the plant defense system. In plants lacking R3 or RPS5 resistance genes, it probably impairs the plant defense system and leads to the bacteria multiplication. In contrast, in plants containing the R3 or RPS5 protein, it is unable to induce disease symptoms, explaining its avirulence name. The 7 kDa product is required for the type-III translocation from Pseudomonas strains to the plant, but are partially dispensable for effector recognition following in planta expression. In infected plants, it acts by cleaving the PBS1 protein, which leads to resistance or disease, depending on the presence or absence of RPS5, respectively (PubMed:11952132, PubMed:17277084). Targets the Arabidopsis kinases PBS1, BIK1, PBL1, PBL2, PBL3, PBL5, PBL7, PBL9 and PBL11 for cleavage in vitro (PubMed:20413097). Can block recognition of AvrB avirulence factor by plant cells by cleaving Arabidopsis RIPK kinase and suppressing Arabidopsis RPM1 activation. Cannot block AvrRpm1-induced activation of RPM1 (PubMed:25625821). {ECO:0000269|PubMed:11952132, ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:25625821}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (7); Chain (2); Helix (7); Lipidation (1); Mutagenesis (5); Site (1); Turn (4) |
Keywords | 3D-structure;Autocatalytic cleavage;Host membrane;Hydrolase;Hypersensitive response elicitation;Lipoprotein;Membrane;Myristate;Protease;Secreted;Thiol protease;Virulence |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10830163}. Host membrane {ECO:0000269|PubMed:10830163}. Note=In infected plant cells, it is membrane-associated. |
Modified Residue | |
Post Translational Modification | PTM: Autocleaved. This function is essential for myristoylation in infected plant cell and for eliciting the plant hypersensitive response. {ECO:0000269|PubMed:10830163}.; PTM: Myristoylation of 28 kDa product in infected plant cells; it mediates the localization to membranes. {ECO:0000305|PubMed:10830163}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1UKF; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 28,704 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |