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Article

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

The Journal of biological chemistry - 4 Jul 2014

Chang Hsin-Yang, Chou Chia-Cheng, Hsu Min-Feng, Wang Andrew H J

Abstract excerpt

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...

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Identifiers

PMID: 24855653
DOI: 10.1074/jbc.M114.575076
PMCID: PMC4081917

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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