EC Number   |
General Information |
Reference |
|---|
   2.7.1.66 | evolution |
prokaryotic diacylglycerol kinase and undecaprenol kinase are the lone members of the prokaryotic diacylglycerol kinase and undecaprenol kinase family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins, including water soluble kinases, and that exhibit an unusual structure and active site architecture. The enzymes show complex structure, forming domain-swapped homotrimers in which each monomer subunit has three transmembrane segments. Members of this family are unrelated to the eukaryotic diacylglycerol kinases and their prokaryotic homologs, encoded by the dgkB gene |
721297 |
| 2.7.1.66 | metabolism |
UDPK activity does not participate in the de novo biosynthetic pathway to undecaprenyl phosphate which does not include free undecaprenol as an intermediate |
721297 |
| 2.7.1.66 | physiological function |
Gram-negative Escherichia coli does not contain high llevels of free undecaprenol, thus has no need for a undecaprenol kinase |
721297 |
| 2.7.1.66 | physiological function |
UDPK is essential for sporulation of Bacillus subtilis |
721297 |
| 2.7.1.66 | physiological function |
UDPK seems to play an analogous role in Gram-positive bacteria, where its importance is evident by the fact that UDPK is essential for biofilm formation by the oral pathogen Streptococcus mutans. Undecaprenol has an unusual function as covalent transmembrane carriers of hydrophilic molecules from the inner to the outer leaflet of the plasma membrane for use in biosynthesis of molecules located in the cell wall or periplasm. UDPK is an important enzyme in Streptococcus mutans required for growth at low pH, for biosynthesis of certain lantibiotics, and for biofilm formation.. It is also a virulence factor for the formation of smooth surface dental caries |
721297 |
