Raw data for the role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS

Data 1<br>Autophosphorylation of LytS.<br>Quantification of phosphorylated LytS bands by NIH Image J. Average of two trials. Data 2<br>Phosphorylation of LytR by acetyl phosphate.<br>Quantification of phosphorylated LytR bands by NIH ImageJ. Data 3<br>Phosphorylation of LytR-N by acetyl phosphate.<br>Quantification of phosphorylated LytR-N bands by NIH ImageJ. Data 4<br>Quantification of LytR bands in native-PAGEs (Figure 6A and B) by NIH Image J. LytR protein was phosphorylated by acetyl phosphate and its dephosphorylation by LytS was monitored by native-PAGE, whereby the phosphorylated dimer LytR becomes monomer after dephosphorylation. The column “corrected” represents the data after correcting for background signal at 0 min, and considering the band labeled “Monomer”, in the absence of LytS and ATP, as 100% unphosphorylated LytR.