Part:BBa_K3955100:Design
Periplasmic serine endoprotease DegP.
- 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
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.