Abstract
The nucleotide sequence of the gtfB gene from Streptococcus mutans GS-5, coding for glucosyltransferase I activity, was determined. The gene codes for a strongly hydrophilic protein with a molecular size of 165,800 daltons. The deduced amino acid sequence revealed a typical gram-positive bacterial signal sequence at the NH2 terminus of the protein and 3.5 direct repeating units (each containing 65 amino acids) at the COOH terminus. Nucleotide sequencing of the region immediately downstream from the gtfB gene revealed the presence of a putative gene coding for an extracellular protein. This open reading frame is partially homologous to the gtfB gene.
MeSH Terms
Amino Acid Sequence
Base Sequence
DNA Restriction Enzymes
DNA, Bacterial/analysis
Genes, Bacterial
Glucosyltransferases/genetics
Sequence Homology, Nucleic Acid
Streptococcus mutans/enzymology,genetics
Chemicals
DNA, Bacterial
1,3-alpha-D-glucan synthase
Glucosyltransferases
DNA Restriction Enzymes
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Shiroza T
Ueda S
Kuramitsu H K
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