PMID:3299373
| Citation |
Bramley, HF and Kornberg, HL (1987) Sequence homologies between proteins of bacterial phosphoenolpyruvate-dependent sugar phosphotransferase systems: identification of possible phosphate-carrying histidine residues. Proc. Natl. Acad. Sci. U.S.A. 84:4777-80 |
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| Abstract |
The DNA sequences for some of the genes involved in the phosphoenolpyruvate-dependent phosphotransferase system (PTS) of Escherichia coli and Salmonella typhimurium have been reported. Comparison of the deduced amino acid sequences of enzyme IIBgi, enzyme IIMtl, and enzyme IIGlc/enzyme IIIGlc, which catalyze the uptake and concomitant phosphorylation of beta-glucosides, mannitol, and glucose, respectively, reveals considerable sequence homology. In particular, the carboxyl-terminal region of enzyme IIBgl is so homologous to the whole of enzyme IIIGlc as to suggest a common function. We postulate that His-547 of enzyme IIBgl receives a phosphate group directly from the cytoplasmic protein HPr and transfers this phosphate to His-306 located in the amino-terminal half of enzyme IIBgl. This latter histidine is conserved in enzyme IIBgl and enzyme IIGlc and, in both proteins, occurs in a region that shows homology with the His-15 region of HPr, which is known to act as the phosphate carrier. An equivalent histidine residue, His-195, is also present in enzyme IIMtl, although here the flanking sequence is different. None of these specified histidine residues is likely to be buried within the membrane. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Escherichia coli/genetics; Histidine/analogs & derivatives; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics; Phosphorylation; Salmonella typhimurium/genetics; Sequence Homology, Nucleic Acid; Software; Species Specificity |
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