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. Interacts physically with plant cell ROC1 (Arabidopsis single-domain cyclophilin) and RIN4. Secreted via type III secretion system (TTSS) (PubMed:14526114). Localized to the plant cell membrane (PubMed:14526114). Autocleaved inside plant cells upon activation by cyclophilin. Cleavage is crucial in subcellular location and in eliciting HR. Inhibited by cyclosporin A (cyclophilin inhibitor). Only naturally present in strain JL1065. The C-terminal cleaved product is sufficient to trigger the RPS2-dependent immune response. Belongs to the peptidase C70 family.