Part:BBa_K3955100
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1252
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 601
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