PMID:8789466
| Citation |
Wu, LF and Mandrand-Berthelot, MA (1995) A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions. Biochimie 77:744-50 |
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| Abstract |
The uptake of peptides is accomplished mainly by a family of homologous oligopeptide or dipeptide transporters in bacteria. Computer-aided sequence analyses expand members of the oligopeptide-binding protein family to nickel and heme permeases and other proteins, including an enzyme hyaluronate synthase. They are involved in human pathogenicity, bacterial virulence, substrate-sensing, bacterial conjugation and bacterial metabolic reactions distinct from nutrient uptake. These homologous proteins are found in both purple bacteria and Gram-positive bacteria, indicating the presence of a common ancestor before the appearance of the two eubacterial phyla. Nevertheless, the pheromone-binding proteins, involved in bacterial conjugation, and the hyaluronate synthase are present only in the low G-C Gram-positive eubacteria subdivision, which suggests that these proteins diverged from the common ancestor after the appearance of this subdivision. |
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| Keywords |
Amino Acid Sequence; Biological Transport; Carrier Proteins; Databases, Factual; Glucuronosyltransferase; Glycosyltransferases; Membrane Proteins; Membrane Transport Proteins; Molecular Sequence Data; Nickel/metabolism; Oligopeptides/metabolism; Phylogeny; Sequence Homology, Amino Acid; Substrate Specificity; Transferases; Xenopus Proteins |
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