Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases
| Autor: | C L, Bouma, S, Roseman |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Base Sequence
Monosaccharide Transport Proteins Molecular Sequence Data Restriction Mapping Membrane Transport Proteins Chitin Polymerase Chain Reaction Bacterial Proteins Amino Acid Sequence Cloning Molecular Phosphorylation Phosphoenolpyruvate Sugar Phosphotransferase System Sequence Alignment Plasmids Vibrio |
| Zdroj: | The Journal of biological chemistry. 271(52) |
| ISSN: | 0021-9258 |
| Popis: | Chitin catabolism by the marine bacterium Vibrio furnissii involves chemotaxis to and transport of N-acetyl-D-glucosamine (GlcNAc) and D-glucose. We report the properties of the respective permeases that complemented E. coli Glc- Man- mutants. Although the V. furnissii Glc-specific permease (55,941 Da) shares 38% identity with E. coli IIGlc (ptsG), it is 67% identical to MalX of the E. coli maltose operon (Reidl, J., and Boos, W. (1991) J. Bacteriol. 173, 4862-4876). An adjacent open reading frame encodes a protein with 52% identity to E. coli MalY. Glc phosphorylation requires only V. furnissii MalX and the accessory phosphoenolpyruvate:glycose phosphotransferase system proteins. The V. furnissii equivalent of IIGlc was not found in the 25,000 transformants screened. The GlcNAc/Glc-specific permease (52,894 Da) shares 47% identity with the N-terminal, hydrophobic domain of E. coli IINag, but is unique among IINag proteins in that it lacks the C-terminal domain and thus requires IIIGlc for sugar fermentation in vivo and phosphorylation in vitro. While there are similarities between the phosphoenolpyruvate:glycose phosphotransferase system of V. furnissii and enteric bacteria, the differences may be important for survival of V. furnissii in the marine environment. |
| Databáze: | OpenAIRE |
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