Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding extracellular dextranase.
The complete nucleotide sequence (3,747 bp) of the dextranase gene (dexA) and flanking regions of the chromosome of Streptococcus mutans Ingbritt (serotype c) were determined. The open reading frame for dexA was 2,550 bp, ending with a stop codon TGA. A putative ribosome-binding site, promoter preceding the start codon, and potential stem-loop structure were identified. The presumed dextranase protein (DexA) consisting of 850 amino acids was estimated to have a molecular size of 94,536 Da and a pI of 4.79. The nucleotide sequence and the deduced amino acid sequences of S. mutans dexA exhibited homologies of 57.8% and 47.0%, respectively, to those of Streptococcus sobrinus dex. The homologous region of dex of S. sobrinus was in the N-terminal half. The C terminus of DexA consisted of a hexapeptide LPQTGD, followed by 7 charged amino acids, 21 amino acids with a strongly hydrophobic character, and a charged hexapeptide tail, which have been reported as a common structure of C termini of not only the surface-associated proteins of Gram-positive cocci but also the extracellular enzymes such as beta-fructosidase of S. mutans and dextranase of S. sobrinus. The DexA protein had no significant homology with the glucosyltransferases, the glucan-binding protein, or the dextranase inhibitor of mutans streptococci.
Igarashi
T
T
Department of Oral Microbiology, Showa University School of Dentistry, Tokyo, Japan.
Yamamoto
A
A
Goto
N
N
D000595:Amino Acid Sequence; D001483:Base Sequence; D003910:Dextranase / Q000737:chemistry / Q000235:genetics*; D005110:Extracellular Space / Q000201:enzymology; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D017421:Sequence Analysis; D017385:Sequence Homology; D013295:Streptococcus mutans / Q000737:chemistry / Q000235:genetics*
D003910:Dextranase