Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling and apoptosis (PubMed:26394407, PubMed:28069818, PubMed:28522607, PubMed:32766249, PubMed:29449376). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as TRADD, TNFRSF1A/TNFR1 and TNFRSF10B/TRAILR2: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:28069818, PubMed:32766249, PubMed:29449376, PubMed:30902834). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab GTPase (Rab1, Rab5 and Rab11), thereby preventing GTPase activity and leading to impaired host vesicular protein transport (PubMed:32504010, PubMed:32974215). Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32432056). L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP Interacts with host TRIM32; without mediating its GlcNAcylation. Secreted via type III secretion system 2 (SPI-2 TTSS) (PubMed:21445262). Localizes to host Golgi apparatus via lipid-binding (PubMed:32504010). Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product. Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. Decreased apoptosis in infected macrophages, characterized by reduced CASP3, CASP8 ans CASP9 caspase activity. Belongs to the glycosyltransferase NleB family.