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). In infected plant cells, the 28 kDa product interacts with PBS1. In infected plant cells, it is membrane-associated. Autocleaved. This function is essential for myristoylation in infected plant cell and for eliciting the plant hypersensitive response. Myristoylation of 28 kDa product in infected plant cells; it mediates the localization to membranes. Belongs to the peptidase C58 family.