Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
CpxP, a stress-combative member of the Cpx regulon.
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CpxP is a periplasmic protein induced by the Cpx system
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CpxP combats extracytoplasmic protein-mediated toxicity
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CpxP mutants are hypersensitive to alkaline pH
The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP.
Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli.
Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP protein.
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CpxP crystal structure at 1.45A shows cap-shaped dimer with polar concave and hydrophobic convex surfaces
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Concave polar surface interacts with CpxA sensor domain
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Hydrophobic cleft on convex surface recognizes misfolded pilus subunits
Structure of the periplasmic stress response protein CpxP.
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
Dynamic interaction between the CpxA sensor kinase and the periplasmic accessory protein CpxP mediates signal recognition in E. coli.
UniProtKB entry for Escherichia coli CpxP (P0AE85)
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Reviewed record summarizes CpxA inhibition, DegP-linked PapE quality control, mild chaperone activity, homodimerization, and periplasmic localization.
"Has mild protein chaperone activity."
Deep research report for Escherichia coli CpxP
Unfolded protein binding annotation review project