Coding
degP

Part:BBa_K3955100

Designed by: Jacob Miefalk   Group: iGEM21_Lund   (2021-09-30)


Periplasmic serine endoprotease DegP.

Periplasmic serine endoprotease DegP (henceforth written DegP) is a protease with amyloid specificity. [1] Bacteria which secrete DegP have been shown to out compete E. coli biofilm formation, while knock out mutants of the same strain may not [2] As curli is a major component of E. coli biofilms and is amyloidic, DegP is a viable curli inhibitor candidate [3], but it may have other potential uses. The protein is a chaperone at low temperatures and a peptidase at higher temperatures. [1,4]

References

1. Krojer T, Sawa J, Schäfer E, Saibil H, Ehrmann M, Clausen T. Structural basis for the regulated protease and chaperone function of DegP. Nature. 2008;453(7197):885-890.

2. Fang K, Jin X, Hong SH. Probiotic Escherichia coli inhibits biofilm formation of pathogenic E. coli via extracellular activity of DegP. Scientific Reports [Internet]. [cited 2021 Oct 9];8(1). Available from: https://search.ebscohost.com/login.aspx?direct=true&db=edselc&AN=edselc.2-52.0-85044277078&site=eds-live&scope=site

3. Barnhart, M. M., & Chapman, M. R. (2006). Curli Biogenesis and Function. Annual Review of Microbiology, 60(1), 131–147. doi:10.1146/annurev.micro.60.080805.142106

4. Spiess C, Beil A, Ehrmann M. A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein. Cell. 1999;97(3):339-347.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 1252
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 601


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