Part:BBa_K1951007
General information about curlin (CsgA protein)
To see an exemple of this biobrick functionality, you can visit our composite part : BBa_K1951010
CsgA is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many Enterobacteriaceae. Curli were first discovered in the late 1980s on Escherichia coli strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of E. coli and Salmonella spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response.
Design summary
Starting from the E.coli flagellin sequence ( http://www.ncbi.nlm.nih.gov/nuccore/EU554560.1 ) we have designed a part to produce this protein in E. coli chassis BBa_K1951010. All forbidden restriction sites have been removed. Codons have been optimized for E.coli to allow a maximal transcription level.
Proof of functionality
This sequence has been tested: placed under the control of a strong promoter with a ribosome binding site the sequence has been validated as functional. For further information, go on the following link : BBa_K1951010 design
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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