Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.

@article{Chang2014ProposedCL,
  title={Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.},
  author={Hsin-Yang Chang and C C Chou and Min-Feng Hsu and Andrew H-J Wang},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 27},
  pages={18719-35}
}
Undecaprenyl pyrophosphate phosphatase (UppP), an integral membrane protein, catalyzes the dephosphorylation of undecaprenyl pyrophosphate to undecaprenyl phosphate, which is an essential carrier lipid in the bacterial cell wall synthesis. Sequence alignment reveals two consensus regions, containing glutamate-rich (E/Q)XXXE plus PGXSRSXXT motifs and a histidine residue, specific to the bacterial UppP enzymes. The predicted topological model suggests that both of these regions are localized near… CONTINUE READING
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