A family of bacterial proteins has been described [1] which groups
transcriptional repressors, sugar kinases and yet uncharacterized open reading
frames. This family, known as ROK (Repressor, ORF, Kinase) currently consist
of:
Xylose operon repressor (gene xylR) in Bacillus subtilis, Lactobacillus
pentosus and Staphylococcus xylosus.
N-acetylglucosamine repressor (gene nagC) from Escherichia coli.
Glucokinase (EC 2.7.1.2) (gene glk) from Streptomyces coelicolor.
Fructokinase (EC 2.7.1.4) (gene scrK or frk) from Pediococcus pentosaceus,
Streptococcus mutans and Zymomonas mobilis.
Hypothetical Escherichia coli protein yajF and HI0182, the corresponding
Haemophilus influenzae protein.
Hypothetical Escherichia coli protein yhcI and HI0144, the corresponding
Haemophilus influenzae protein.
A hypothetical protein in nagH 5'region from Clostridium perfringens.
The repressor proteins (xylR and nagC) from this family possess a N-terminal
region not present in the sugar kinases and which contains an helix-turn-helix
DNA-binding motif. The domain common to all these proteins consists of about
300 residues. It is not highly conserved, but we could define a pattern
centered on a glycine-rich region in the central part of the domain.
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