| Title: | A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions |
| Author(s): | Wu LF; Mandrand-Berthelot MA; |
| Address: | "Institut National des Sciences Appliquees, Villeurbanne, France" |
| DOI: | 10.1016/0300-9084(96)88192-2 |
| ISSN/ISBN: | 0300-9084 (Print) 0300-9084 (Linking) |
| 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" |
| Keywords: | "Amino Acid Sequence Biological Transport *Carrier Proteins Databases, Factual Glucuronosyltransferase *Glycosyltransferases Hyaluronan Synthases *Membrane Proteins *Membrane Transport Proteins Molecular Sequence Data Nickel/metabolism Oligopeptides/*metab;" |
| Notes: | "MedlineWu, L F Mandrand-Berthelot, M A eng France 1995/01/01 Biochimie. 1995; 77(9):744-50. doi: 10.1016/0300-9084(96)88192-2" |
