Abstract
The nucleotide sequence of the fruA gene, the terminal gene in the fructose operon of Rhodobacter capsulatus, is reported. This gene codes for the fructose permease (molecular weight, 58,575; 578 aminoacyl residues), the fructose enzyme II (IIFru) of the phosphoenolpyruvate-dependent phosphotransferase system. The deduced aminoacyl sequence of the encoded gene product was found to be 55% identical throughout most of its length with the fructose enzyme II of Escherichia coli, with some regions strongly conserved and others weakly conserved. Sequence comparisons revealed that the first 100 aminoacyl residues of both enzymes II were homologous to the second 100 residues, suggesting that an intragenic duplication of about 300 nucleotides had occurred during the evolution of IIFru prior to divergence of the E. coli and R. capsulatus genes. The protein contains only two cysteyl residues, and only one of these residues is conserved between the two proteins. This residue is therefore presumed to provide the active-site thiol group which may serve as the phosphorylation site. IIFru was found to exhibit regions of homology with sequenced enzymes II from other bacteria, including those specific for sucrose, beta-glucosides, mannitol, glucose, N-acetylglucosamine, and lactose. The degree of evolutionary divergence differed for different parts of the proteins, with certain transmembrane segments exhibiting high degrees of conservation. The hydrophobic domain of IIFru was also found to be similar to several uniport and antiport transporters of animals, including the human and mouse insulin-responsive glucose facilitators. These observations suggest that the mechanism of transmembrane transport may be similar for permeases catalyzing group translocation and facilitated diffusion.