E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP (PubMed:27572974). Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria (PubMed:27572974). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:27572974). 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, probably due to interactions of the leucine-rich repeat domain with the catalytic domain. Is activated upon binding to a substrate protein. Interacts with human RBCK1/HOIL-1 and RNF31/HOIP components of the LUBAC complex. Secreted via Mxi-Spa type III secretion system (TTSS), and delivered into the host cytoplasm. The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins. Belongs to the LRR-containing bacterial E3 ligase family.