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 TRADD and, to a lower extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (By similarity). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2, leading to inhibit NF-kappa-B signaling (By similarity). Catalyzes GlcNAcylation of host tubulin-folding cofactor TBCB, thereby promoting microtubule stability (By similarity). Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (By similarity). L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP Protein-arginine N-acetylglucosaminyltransferase activity is inhibited by 100066N compound (flavone analog) and 102644N compound (a substituted isoxazole). Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 TTSS). 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. Reduced virulence. Belongs to the glycosyltransferase NleB family. Truncated N-terminus.