Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues (PubMed:10564523, PubMed:18005683, PubMed:16611232, PubMed:24248594). This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (PubMed:10564523, PubMed:18005683, PubMed:16611232, PubMed:24248594). Can ubiquitinate ubiquitin, giving rise to polyubiquitin chains (in vitro) (PubMed:18005683). Polyubiquitinates host PKN1, leading to its proteasomal degradation (PubMed:16611232, PubMed:24248594). Down-modulates production of host pro-inflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression; this depends only partially on its E3 ubiquitin-protein ligase activity (PubMed:12819095). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Exists in an autoinhibited state in the absence of substrate protein, due to interactions of the leucine-rich repeat domain with the catalytic domain. Is activated upon binding to a substrate protein. Interacts (via leucine-rich repeat region) with host PKN1 (via the second REM repeat). Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 TTSS), and delivered into the host cytoplasm. Localizes predominantly to the host nucleus. Transcription is maximal in the late logarithmic phase of growth. Expression levels are similar in the intracellular and extracellular environments. The LRR (leucine-rich repeat) domain mediates interaction with host PKN1 and inhibition of NF-kappa-B-dependent gene expression. Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. Belongs to the LRR-containing bacterial E3 ligase family.