Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TNFRSF1A and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Has preference for host FADD as substrate compared to TNFRSF1A and RIPK1. Also acts on host proteins without a death domain: catalyzes GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2 and TRAF3, leading to inhibit NF-kappa-B signaling and type I interferon production, respectively. Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB. Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins 