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PMID: 3397182 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Sequence analysis of the Streptococcus mutans scrB gene.

Infection and immunity ·Vol. 56 ·No. 8 ·1988-08-00 ·Pages 1956-60

Sato Y, Kuramitsu HK

Abstract

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.

MeSH Terms
Amino Acid Sequence Base Sequence Codon DNA, Bacterial/genetics Genes Genes, Bacterial Glycoside Hydrolases/genetics Molecular Sequence Data Sequence Homology, Nucleic Acid Streptococcus mutans/enzymology,genetics beta-Fructofuranosidase
Chemicals
Codon DNA, Bacterial Glycoside Hydrolases beta-Fructofuranosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sato Y
Department of Microbiology-Immunology, Northwestern University Medical-Dental Schools, Chicago, Illinois 60611.
Kuramitsu H K
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1988-08-00
Pages
1956-60
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC259507
Subset
IM
Grants
NIDCR NIH HHS · DE-03258 · United States
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