Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase.

@article{Touz2008SubstrateSA,
  title={Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase.},
  author={Thierry Touz{\'e} and Didier Blanot and Dominique Mengin-Lecreulx},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 24},
  pages={16573-83}
}
The synthesis of the lipid carrier undecaprenyl phosphate (C(55)-P) requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate (C(55)-PP). The latter lipid is synthesized de novo in the cytosol and is also regenerated after its release from the C(55)-PP-linked glycans in the periplasm. In Escherichia coli the dephosphorylation of C(55)-PP was shown to involve four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG… CONTINUE READING