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:28522607). 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 (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (PubMed:28522607). 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. Belongs to the glycosyltransferase NleB family.