Lf. Wu et Ma. Mandrandberthelot, A FAMILY OF HOMOLOGOUS SUBSTRATE-BINDING PROTEINS WITH A BROAD RANGE OF SUBSTRATE-SPECIFICITY AND DISSIMILAR BIOLOGICAL FUNCTIONS, Biochimie, 77(9), 1995, pp. 744-750
The uptake of peptides is accomplished mainly by a family of homologou
s oligopeptide or dipeptide transporters in bacteria. Computer-aided s
equence analyses expand members of the oligopeptide-binding protein fa
mily to nickel and heme permeases and other proteins, including an enz
yme hyaluronate synthase. They are involved in human pathogenicity, ba
cterial virulence, substrate-sensing, bacterial conjugation and bacter
ial metabolic reactions distinct from nutrient uptake. These homologou
s proteins are found in both purple bacteria and Gram-positive bacteri
a, indicating the presence of a common ancestor before the appearance
of the two eubacterial phyla. Nevertheless, the pheromone-binding prot
eins, involved in bacterial conjugation, and the hyaluronate synthase
are present only in the low G-C Cram-positive eubacteria subdivision,
which suggests that these proteins diverged from the common ancestor a
fter the appearance of this subdivision.