Difference between revisions of "Part:BBa K1486000"
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===Activity Regulation===
 
===Activity Regulation===
 
The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins.
 
The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins.
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It is also activated by by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion. <ref>“The Cpx Two-Component Signal Transduction Pathway of Escherichia Coli Regulates Transcription of the Gene Specifying the Stress-Inducible Periplasmic Protease, DegP.” n.d. Www.uniprot.org. https://www.uniprot.org/citations/7883164.
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It is also activated by by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion. <ref>“The Cpx Two-Component Signal Transduction Pathway of Escherichia Coli Regulates Transcription of the Gene Specifying the Stress-Inducible Periplasmic Protease, DegP.” n.d. Www.uniprot.org. https://www.uniprot.org/citations/7883164.</ref>
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Cpx two-component system is activated at pH 8.0; in a degP deletion mutant activation is halved,. The CpxA kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition .
 
Cpx two-component system is activated at pH 8.0; in a degP deletion mutant activation is halved,. The CpxA kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition .
  

Revision as of 23:03, 30 July 2021

CpxR coding region

CpxR is a transciption factor that dimerizes and becomes active when phosphorylated by the transmembrane histidine kinase CpxA. CpxA becomes active when the bacterial cell is submitted to different kinds of shock (pH, temperature, pressure, protein misfolding in the inter-membrane space...).

Information contributed by City of London UK (2021)

Part information is collated here to help future users of the BioBrick registry.

Metadata:

  • Group: City of London UK 2021
  • Author: Julian Chen
  • Summary: Added information collated from existing scientific studies

It is a response regulator of the regulatory system 'CpxA/CpxR', which is a 2 component regulatory system. It responds to the envelope stress response with the activation of the downstream genes including cpxP, degP, dsbA and ppiA. [1] [2] It is required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation and when induced upon cell surface binding, it induces the genes it controls. [3] It also binds and activates transcription from the degP promoter-the binding is enhanced by phosphorylation. This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E, as well as that of CpxP protein. Other downstream effectors may include SrkA. Cite error: Closing </ref> missing for <ref> tag Cpx two-component system is activated at pH 8.0; in a degP deletion mutant activation is halved,. The CpxA kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition .



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Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 61
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 472
  • 1000
    COMPATIBLE WITH RFC[1000]


  1. ↑ “The Cpx Two-Component Signal Transduction Pathway of Escherichia Coli Regulates Transcription of the Gene Specifying the Stress-Inducible Periplasmic Protease, DegP.” n.d. Www.uniprot.org. Accessed July 30, 2021. https://www.uniprot.org/citations/7883164.
  2. ↑ “Transduction of Envelope Stress in Escherichia Coli by the Cpx Two-Component System.” n.d. Www.uniprot.org. https://www.uniprot.org/citations/9401031.
  3. ↑ “Surface Sensing and Adhesion of Escherichia Coli Controlled by the Cpx-Signaling Pathway.” n.d. Www.uniprot.org. Accessed July 30, 2021. https://www.uniprot.org/citations/11830644