Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:30327479). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (PubMed:32974215). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (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 the type III secretion system (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. Reduced virulence. Belongs to the glycosyltransferase NleB family.