InterPro domain: IPR005218

The Escherichia coli member of this family, YegS, has been purified and shown to have phosphatidylglycerol kinase activity [ 1 ]. DagK from Bacillus subtilis catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine [ 2 ].

1. Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. J. Biol. Chem. 282, 19644-52
2. Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis. J. Biol. Chem. 282, 21738-45