Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme.
The nucleotide sequence of the Streptococcus mutans GS-5 gtfD gene coding for the glucosyltransferase which synthesizes water-soluble glucan (GTF-S) has been determined. The complete gene contains 4293 base pairs and the unprocessed protein is composed of 1430 amino acids with a molecular mass of 159814 Da. The amino terminus of the unprocessed protein resembles the signal sequences of other extracellular proteins secreted by S. mutans and that of the GTF-I secreted by Streptococcus downei. In addition, the GTF-S protein exhibits high amino acid similarity with the strain GS-5 enzymes responsible for insoluble glucan synthesis (GTF-I, GTF-SI) previously isolated and sequenced in this laboratory. These results indicate that all three gtf genes evolved from a common ancestral gene.
Honda
O
O
Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611.
Kato
C
C
Kuramitsu
H K
HK
D000595:Amino Acid Sequence; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D005964:Glucosyltransferases / Q000235:genetics*; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid; D013295:Streptococcus mutans / Q000201:enzymology* / Q000235:genetics
D004269:DNA, Bacterial; D021382:Protein Sorting Signals; C036655:1,3-alpha-D-glucan synthase; D005964:Glucosyltransferases