EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.7.65 | more |
pseudo-phosphorylation by beryllium fluoride (BeF3-) modification at residue Asp53 in Rec-domain (D1), tightens dimer |
682885 |
| 2.7.7.65 | phosphoprotein |
- |
705162 |
| 2.7.7.65 | phosphoprotein |
enzyme is activated by phosphorylation of residue D53. In vitro, enzyme PleD can be activated by beryllium fluoride, resulting in dimerization and synthesis of cyclic diguanylate |
680826 |
| 2.7.7.65 | phosphoprotein |
localization of response regulator PleD to the stalked pole requires its activation by phosphorylation and is dependent on the polar kinases DivJ and PleC |
680007 |
| 2.7.7.65 | phosphoprotein |
phosphorylation is required for catalytic activity |
680449 |
| 2.7.7.65 | phosphoprotein |
when activated by phosphorylation, yellow fluorescent protein (YFP)-tagged WspR forms clusters that are visible in individual cells by fluorescence microscopy. Unphosphorylated WspR is diffuse in cells and not visible. In general, increased cluster formation correlates with increased in vivo and in vitro diguanylate cyclase activities of variants. In addition, WspR specific activity is strongly concentration dependent in vitro, and the effect of the protein concentration on diguanylate cyclase activity is magnified when WspR is treated with the phosphor analog beryllium fluoride. Cluster formation appears to be an intrinsic property of phosphorylated WspR |
738962 |
