The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:4919472). This system is involved in N-acetylglucosamine transport (PubMed:4919472). It can also transport and phosphorylate the antibiotic streptozotocin (PubMed:161156). Could play a significant role in the recycling of peptidoglycan (PubMed:19617367). N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) = L-histidyl-[protein] + N-acetyl-D-glucosamine 6-phosphate(in) P-chloromercuribenzoate inhibits the accumulation of both N-acetyl-D-glucosamine and antibiotic streptozotocin (2-deoxy-2-(3-methyl-3-nitrosoureido)-D-glucopyranose). N-acetyl-D-glucosamine is a competitive inhibitor for the uptake of streptozotocin. Induced by N-acetylglucosamine-6-phosphate and repressed by NagC. The PTS EIIC type-1 domain forms the PTS system translocation channel and contains the specific substrate-binding site. The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain. The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-1 domain. Cells lacking nagE and nagA reduce by 50% the amount of GlcNAc6P. Together with the mutations of the genes of the peptidoglycan recycling pathway (ampG, anmK, murQ, nagK and nagZ), the accumulation of GlcNAc6P is eliminated.