EC Number   |
General Information |
Reference |
|---|
  2.7.8.47 | physiological function |
deletion mutants of primase tarK and polymerase tarL, respectively, are viable, each gene is individually dispensable. Mutants of tarK and tarL are not compromised in growth or cell wall teichoic acid levels. A tarK and tarL double deletion cannot be created in a wild-type background |
-, 740613 |
| 2.7.8.47 | physiological function |
polymerase TarL catalyzes chain extension of wall teichoic acid intermediates primed by TarF. TarL is unable to use glycerol-phosphate primed intermediates to create the polymer, but TarLBs reacts with the ribitol-phosphate-primed substrate and adds multiple polyribitolphosphate subunits |
-, 740298 |
| 2.7.8.47 | physiological function |
TarK is a bifunctional enzyme that catalyzes both ribitol phosphate priming and polymerization, reactions of EC 2.7.18.46 and 2.7.8.47. TarK can replace polymerase TarL provided that it is sufficiently expressed. TarK directs the synthesis of a polyribitol-containing teichoic acid K-WTA. The biosynthesis of K-WTA is repressed by the accessory gene regulator (agr) system |
-, 740612 |
