Detail Information for IndEnz0002005136
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