The mannitol-specific enzyme II (mtIA) gene and the mtIR gene of the PTS of Streptococcus mutans

Allen L. Honeyman, Roy Curtiss

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


The phosphoenolpyruvate-dependent phosphotransferase system (PTS) is widely found among Gram-positive bacteria. It is the major source of carbohydrate transport in the dental pathogen Streptococcus mutans. The transported carbohydrates are fermented to produce large amounts of lactic acid which initiates dental caries. The authors have isolated the S. mutans gene for the mannitol-specific Enzyme II (EII) component of the PTS, mtlA, and the adjacent mtlR gene, which is located in the same operon. The mtlR gene is located between mtlA and the genes mtlF and mtlD. The nucleotide sequence of the mtlA and mtlR loci has been determined. The deduced mtlA gene product of S. mutans consists of 589 amino acids with a molecular mass of 62·0kDa. It exhibits similarity with the mtlA gene products from other organisms. However, the similarity between these proteins is generally restricted to the 470 amino-terminal residues of the S. mutans protein. This region would correspond to the EIICB domains of the PTS. The authors have previously shown that the S. mutans mtlF gene product exhibits 76.6% similarity to the carboxyl-terminal 143 amino acids of the Escherichia coli mtlA product and that the mtlF gene encodes the EIIA domain of the PTS. Thus, the genes that encode the EIICB and the EIIA domains are separated by approximately 2250 bp. In many organisms, all of the EII domains may be fused together to form one molecule. The fact that these domains are separated by this distance in S. mutans supports the hypothesis that various functional domains of the PTS have been rearranged during evolution. The sequence of the 119 carboxyl-terminal amino-acids of the S. mutans mltA gene product also displays homology to the carboxyl-terminal end of the EIIB domain of various mannitol PTSs. Thus, this domain may have been duplicated in S. mutans during evolution of the operon. The mtlR gene is located in the same operon structure as mtlA but these loci are separated by an intragenic space. The precise 5' end of the mtlR locus cannot be determined either by in vitro transcription-translation assays or based upon nucleotide sequence analysis because of the apparent lack of a ribosome-binding site preceding the gene. The deduced mtlR gene product, which consists of approximately 650 amino acids with a molecular mass of 75·3kDa, exhibits limited similarity to several potential transcriptional regulators. However, the exact function of this locus is currently unknown.

Original languageEnglish (US)
Pages (from-to)1565-1572
Number of pages8
Issue number7
StatePublished - Jul 2000


  • Mannitol
  • Phosphoenolypruvate-dependent phosphotransferase system
  • Streptococcus mutans

ASJC Scopus subject areas

  • Microbiology


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