Coding
degP

Part:BBa_K3955100:Design

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


Periplasmic serine endoprotease DegP.


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


Design Notes

Codon optimized for Limosilactobacillus reuteri.


Source

The source is the amino acid sequence found in uniprot for Periplasmic serine endoprotease DegP (https://www.uniprot.org/uniprot/P0C0V0) converted into an nucleotide sequence. That nucleotide sequence was then codon optimized for L. reuteri.

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.