A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions
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 synt...
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Veröffentlicht in: | Biochimie 1995, Vol.77 (9), p.744-750 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 0300-9084 1638-6183 |
DOI: | 10.1016/0300-9084(96)88192-2 |