Difference between revisions of "Part:BBa K3861000"
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| − | Secretion signal and chaperone for secretion of a POI though the SPI-1 T3SS of <i>Salmonella</i> Typhimurium<sup>1</sup>. SptP167 is shortened to the first 167 amino acids but contains the secretion signal and the sicP binding domain needed for functional secretion. SicP is the SptP specific chaperone<sup>2</sup>. | + | Secretion signal and chaperone for secretion of a POI though the SPI-1 T3SS of <i>Salmonella</i> Typhimurium<sup>1</sup>. SptP167 is shortened to the first 167 amino acids but contains the secretion signal and the sicP binding domain needed for functional secretion. SicP is the SptP specific chaperone that unfolds the POI secondary structure for SPI T3SS mediated export <sup>2</sup>. |
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Revision as of 16:31, 19 October 2021
PlldR-sicP-sptP
Secretion signal and chaperone for secretion of a POI though the SPI-1 T3SS of Salmonella Typhimurium1. SptP167 is shortened to the first 167 amino acids but contains the secretion signal and the sicP binding domain needed for functional secretion. SicP is the SptP specific chaperone that unfolds the POI secondary structure for SPI T3SS mediated export 2.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 78
Illegal NheI site found at 101 - 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
1. Lee, S. H. & Galán, J. E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51, 483–495 (2004). 2. Stebbins, C. E. & Galán, J. E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414, 77–81 (2001).