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 that contain 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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The lactate-inducible lldR promoter (<a href="https://parts.igem.org/Part:BBa_K1847008">BBa_K1847008</a>) fused to RBS(SicP)-sicP-sptP (<a href="https://parts.igem.org/Part:BBa_K3861028">BBa_K3861028</a>). SicP-SptP is the 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 that contain 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-1 T3SS mediated export.<sup>2</sup>
 
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Latest revision as of 15:55, 21 October 2021


PlldR-sicP-sptP

The lactate-inducible lldR promoter (BBa_K1847008) fused to RBS(SicP)-sicP-sptP (BBa_K3861028). SicP-SptP is the secretion signal and chaperone for secretion of a POI though the SPI-1 T3SS of Salmonella Typhimurium.1 SptP167 is shortened to the first 167 amino acids that contain 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-1 T3SS mediated export.2

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 78
    Illegal NheI site found at 101
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE 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).