PUL ID

PUL0197

PubMed

17233733, FEMS Microbiol Lett. 2007 Jan;266(2):218-23. doi: 10.1111/j.1574-6968.2006.00522.x.

Characterization method

gene deletion mutant and growth assay

Genomic accession number

NC_004350.2

Nucelotide position range

1488085-1497922

Substrate

maltose

Loci

SMU_1564-SMU_1571

Species

Streptococcus mutans/1309

Degradation or Biosynthesis

degradation

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 2277 (-) CAZyme: GT35 Yes
malQ 2249 - 3778 (-) CAZyme: GH77 Yes
- 3893 - 4912 (-) TF: DBD-Pfam|LacI,DBD-SUPERFAMILY|0036955 Yes
- 5159 - 6406 (+) TC: gnl|TC-DB|Q8DT28|3.A.1.1.27 Yes
- 6483 - 7844 (+) TC: gnl|TC-DB|Q8DT27|3.A.1.1.27 Yes
- 7844 - 8680 (+) TC: gnl|TC-DB|Q8DT26|3.A.1.1.27 Yes
ugpC 8705 - 9838 (+) TC: gnl|TC-DB|Q8DT25|3.A.1.1.27 Yes

PUL ID

PUL0197

PubMed

17233733, FEMS Microbiol Lett. 2007 Jan;266(2):218-23. doi: 10.1111/j.1574-6968.2006.00522.x.

Title

Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans.

Author

Kilic AO, Honeyman AL, Tao L

Abstract

Sugar metabolism by Streptococcus mutans is associated with tooth decay. The most abundant sugars in the human diet are sucrose and maltose, a derivative of starch. Previously, we reported a binding protein-dependent transport system (msm) in S. mutans that transports sucrose and maltose, but its associated enzymes do not metabolize maltose. By searching the S. mutans genomic sequence for a maltose system (mal), we found a gene cluster encoding proteins with homology to those of msm and the Escherichia coli maltose system. Mutants were constructed by deleting msm or mal, or both, and tested for sugar utilization. Deletion of the mal system diminished the ability of S. mutans to ferment maltose, but deletion of only the mal transporter genes or msm showed reduced utilization of chromogenic maltosides. Maltose, sucrose, glucose, fructose, mannose, and N-acetyl glucosamine inhibited utilization of chromogenic maltosides by the wild-type strain and mutants. In conclusion, the two binding protein-dependent systems in S. mutans appear to transport collaboratively their common substrate sugars, notably sucrose and maltose.