Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the first ribitol unit to the disaccharide linker of the teichoic acid.
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The enzyme appears in viruses and cellular organisms
Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the first ribitol unit to the disaccharide linker of the teichoic acid.
TarK functions to prime the wall teichoic acid intermediate for chain extension by TarL. TarK is only able to accept lipid-diphospho-GlcNAc-ManNAc-GroP, the TagB product, as a substrate
TarK functions to prime the wall teichoic acid intermediate for chain extension by TarL. TarK is only able to accept lipid-diphospho-GlcNAc-ManNAc-GroP, the TagB product, as a substrate
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 directs the synthesis of a polyribitol-containing teichoic acid K-WTA
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 directs the synthesis of a polyribitol-containing teichoic acid K-WTA
TarK functions to prime the wall teichoic acid intermediate for chain extension by TarL. TarK is only able to accept lipid-diphospho-GlcNAc-ManNAc-GroP, the TagB product, as a substrate
TarK functions to prime the wall teichoic acid intermediate for chain extension by TarL. TarK is only able to accept lipid-diphospho-GlcNAc-ManNAc-GroP, the TagB product, as a substrate
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
in Staphylococcus aureus, a the tarK ortholog is missing from the analyzed strains. It may be functionally replaced by one of the two tarL genes or be compensated for by the extra copy of tarL
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
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
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
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Enzyme Nomenclature
2.7.8.46 teichoic acid ribitol-phosphate primase
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