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. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is responsible for growth on MurNAc as the sole source of carbon and energy. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring. N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-phosphate(in) Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Also up-regulated by the cAMP receptor protein crp via the binding of crp-cAMP to a class I site upstream of the murQ promoter. Repressed by MurR in the absence of MurNAc 6-phosphate. The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain. The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. The PTS domain EIIA required for activity was shown to be the crr-encoded enzyme IIA-glucose, EIIA-Glc.