Difference between revisions of "Part:BBa K3861028"

Line 1: Line 1:
  
 
__NOTOC__
 
__NOTOC__
<partinfo>BBa K3861028 short</partinfo>
+
<partinfo>BBa_K3861028 short</partinfo>
  
 
<html>
 
<html>
Line 12: Line 12:
 
<!-- -->
 
<!-- -->
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
<partinfo>BBa K3861028SequenceAndFeatures</partinfo>
+
<partinfo>BBa_K3861028SequenceAndFeatures</partinfo>
  
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  
 
===Functional Parameters===
 
===Functional Parameters===
<partinfo>BBa K3861028parameters</partinfo>
+
<partinfo>BBa_K3861028parameters</partinfo>
 
<!-- -->
 
<!-- -->
 
=='''References'''==
 
=='''References'''==

Revision as of 20:43, 20 October 2021


RBS(SicP)-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 No part name specified with partinfo tag.


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).