Difference between revisions of "Part:BBa K3861028"

 
Line 1: Line 1:
  
 +
__NOTOC__
 +
<partinfo>BBa_K3861000 short</partinfo>
 +
 +
<html>
 +
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>
 +
</html>
 +
 +
<!-- Add more about the biology of this part here
 +
===Usage and Biology===
 +
 +
<!-- -->
 +
<span class='h3bb'>Sequence and Features</span>
 +
<partinfo>BBa_K3861000 SequenceAndFeatures</partinfo>
 +
 +
 +
<!-- Uncomment this to enable Functional Parameter display
 +
===Functional Parameters===
 +
<partinfo>BBa_K3861000 parameters</partinfo>
 +
<!-- -->
 +
=='''References'''==
 +
1. Lee, S. H. & Galán, J. E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51, 483–495 (2004).
 +
<br>
 +
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).

Revision as of 20:38, 20 October 2021


PlldR-sicP-sptP

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 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).