The transport of alpha-methylglucoside (MG) in the wild type cells of Escherichia coli K12 and the isogenic mutant strains, defective in the activity of phosphoenolpyruvate: sugar phosphotransferase system components was studied. It was shown that the enzyme IIB' in the absence of enzyme I and HPr is able to transport MG into the cells by a "facilitated" diffusion mechanism. Compounds which dissipate the energy of membrane protone potential such as NaN3, carbonylcyanide-m-chlorophenylhydrasone, dicyclohexylcarbodiimide, enhance the utilization of MG by the wild-type cells. However, the cells retaining intact enzyme IIB' but deficient in the phospho approximately HPr-generating system, were not sensitive to the action of poisons. The cells possessing the intact phospho HPr-generating system and inactive enzyme IIB' are also unaffected by the poisons. It seems that these results do not confirm the hypothesis of the direct delta mu H+ involvement in the regulation of transmembrane phosphorylation. The hypothesis is postulated that the energy metabolism inhibitors influence the phosphatase activity of factor III of the phosphotransferase system. The present data are well explained by this hypothesis.