A glucosyltransferase (GTF) gene, designated gtfL, from Streptococcus
salivarius was cloned and expressed in Escherichia coli and its nucleo
tide sequence determined. The GTF-L enzyme catalysed the synthesis of
water-insoluble glucan in a primer-independent manner. The nucleotide
sequence and derived amino acid sequence of GTF-L were similar in size
and domain structure to previously sequenced glucosyltransferases. Ho
wever, a 464-bp region of high variability was identified which could
be selectively amplified from strains of S. salivarius by the polymera
se chain reaction and could therefore form the basis for species ident
ification. No sequence-specific motifs related to the solubility and l
inkage of the glucan product or its need for a dextran primer could be
ascertained.