Sequence analysis of the Streptococcus mutans scrB gene.
The complete nucleotide sequence of the Streptococcus mutans GS-5 scrB gene coding for sucrose-6-phosphate hydrolase activity was determined. A potential ribosome-binding site as well as promoter sequences were identified upstream from the gene. The deduced amino acid sequence of the enzyme suggested a molecular weight of 51,750, which is similar to that estimated for the enzyme isolated from strain GS-5. The enzyme is slightly acidic, with a pI of 5.9, and is a relatively hydrophilic protein. The nucleotide and amino acid sequences of the enzyme showed significant homology with those of the sacA protein from Bacillus subtilis. In addition, a region of amino acid homology with the S. mutans fructosyltransferase and B. subtilis levansucrase proteins was also detected.
Sato
Y
Y
Department of Microbiology-Immunology, Northwestern University Medical-Dental Schools, Chicago, Illinois 60611.
Kuramitsu
H K
HK
D000595:Amino Acid Sequence; D001483:Base Sequence; D003062:Codon; D004269:DNA, Bacterial / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D006026:Glycoside Hydrolases / Q000235:genetics*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013295:Streptococcus mutans / Q000201:enzymology / Q000235:genetics*; D043324:beta-Fructofuranosidase
D003062:Codon; D004269:DNA, Bacterial; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase