Difference between revisions of "Part:BBa K283007"

Latest revision as of 12:14, 21 October 2009

sp-eGFP-streptavidin-AIDAc

Autotransporters are synthesized as pre-proproteins with modular organization. A C-terminal membrane-embedded domain promotes secretion of parts of the protein across the outer membrane and is composed of a β-barrel and a α-helix spanning its lumen. The adhesion involved in diffuse adherence (AIDA-I) is a monemeric autotransporter that has been extensively studied. The cleavage of the autotransporter adhesion involve in diffuse adherence (AIDA-I) of Escherichia coli yields a membrane embedded fragments, AIDAc, and an extracellular fragments, the mature AIDA-I adhesion. In this part, AIDAc directs the fusion protein sp-eGFP-streptavidin-AIDAc (sp means signal sequence) to the outer membrane of the bacteria by the AIDA-I autotransporter pathway. The surface localization of sp-eGFP-streptavidin-AIDAc was demonstrated in our wiki website.In addition, the restriction of autotransporters to the pole is dependent on the presence of a complete lipopolysaccharide (LPS), consistent with known effects of LPS composition on membrane fluidity.This part does not pose any biological threat.

Sequence and Features

Assembly Compatibility:

10
INCOMPATIBLE WITH RFC[10]
Illegal EcoRI site found at 181
Illegal EcoRI site found at 1675
Illegal EcoRI site found at 2371
Illegal PstI site found at 1723
Illegal PstI site found at 2309
12
INCOMPATIBLE WITH RFC[12]
Illegal EcoRI site found at 181
Illegal EcoRI site found at 1675
Illegal EcoRI site found at 2371
Illegal PstI site found at 1723
Illegal PstI site found at 2309
21
INCOMPATIBLE WITH RFC[21]
Illegal EcoRI site found at 181
Illegal EcoRI site found at 1675
Illegal EcoRI site found at 2371
Illegal BamHI site found at 17
Illegal BamHI site found at 949
Illegal BamHI site found at 2573
Illegal XhoI site found at 2779
23
INCOMPATIBLE WITH RFC[23]
Illegal EcoRI site found at 181
Illegal EcoRI site found at 1675
Illegal EcoRI site found at 2371
Illegal PstI site found at 1723
Illegal PstI site found at 2309
25
INCOMPATIBLE WITH RFC[25]
Illegal EcoRI site found at 181
Illegal EcoRI site found at 1675
Illegal EcoRI site found at 2371
Illegal PstI site found at 1723
Illegal PstI site found at 2309
Illegal AgeI site found at 991
Illegal AgeI site found at 1042
1000
COMPATIBLE WITH RFC[1000]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K283007 short</partinfo>
-Autotransporters are synthesized as pre-proproteins with modular organization. A C-terminal membrane-embedded domain promotes secretion of parts of the protein across the outer membrane and is composed of a &#946;-barrel and a &#945;-helix spanning its lumen. The adhesion involved in diffuse adherence (AIDA-I) is a monemeric autotransporter that has been extensively studied. The cleavage of the autotransporter adhesion involve in diffuse adherence (AIDA-I) of Escherichia coli yields a membrane embedded fragments, AIDAc, and an extracellular fragments, the mature AIDA-I adhesion. In this part, AIDAc directs the fusion protein sp-eGFP-streptavidin-AIDAc (sp means signal sequence) to the outer membrane of the bacteria by the AIDA-I autotransporter pathway.  The surface localization of sp-eGFP-streptavidin-AIDAc was demonstrated in our wiki website.In addition, the restriction of autotransporters to the pole is dependent on the presence of a complete lipopolysaccharide (LPS), consistent with known effects of LPS composition on membrane fluidity.
+Autotransporters are synthesized as pre-proproteins with modular organization. A C-terminal membrane-embedded domain promotes secretion of parts of the protein across the outer membrane and is composed of a &#946;-barrel and a &#945;-helix spanning its lumen. The adhesion involved in diffuse adherence (AIDA-I) is a monemeric autotransporter that has been extensively studied. The cleavage of the autotransporter adhesion involve in diffuse adherence (AIDA-I) of Escherichia coli yields a membrane embedded fragments, AIDAc, and an extracellular fragments, the mature AIDA-I adhesion. In this part, AIDAc directs the fusion protein sp-eGFP-streptavidin-AIDAc (sp means signal sequence) to the outer membrane of the bacteria by the AIDA-I autotransporter pathway.  The surface localization of sp-eGFP-streptavidin-AIDAc was demonstrated in our wiki website.In addition, the restriction of autotransporters to the pole is dependent on the presence of a complete lipopolysaccharide (LPS), consistent with known effects of LPS composition on membrane fluidity.This part does not pose any biological threat.