Evidence for the evolutionary relatedness of the proteins of the bacterial phosphoenolpyruvate:Sugar phosphotransferase system

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Abstract
The phosphoenolpyruvate:sugar phosphotransferase system (PTS) found in enteric bacteria is a complex enzyme system consisting of a non-sugar-specific phospho-transfer protein called Enzyme I, two small non-sugar-specific phosphocarrier substrates of Enzyme I, designated HPr and FPr, and at least 11 sugar-specific Enzymes II or Enzyme II-III pairs which are phosphorylated at the expense of phospho-HPr or phospho-FPr. In this communication, evidence is presented which suggests that these proteins share a common evolutionary origin and that a fructose-specific phosphotransferase may have been the primordial ancestor of them all. The evidence results from an evaluation of (1) PTS protein sequence data; (2) structural analysis of operons encoding proteins of the PTS; (3) genetic regulatory mechanisms controlling expression of these operons; (4) enzymatic characteristics of the PTS systems; (5) immunological cross reactivities of these proteins; (6) comparative studies of phosphotransferase systems from evolutionarily divergent bacteria; (7) the nature of the phosphorylated protein intermediates; (8) molecular weight comparisons among the different Enzymes II and Enzyme II-III pairs; and (9) interaction studies involving different PTS protein constituents. The evidence leads to a unifying theory concerning the evolutionary origin of the system, explains many structural, functional, and regulatory properties of the phosphotransferase system, and leads to specific predictions which should guide future research concerned with genetic, biochemical, and physiological aspects of the system.