Difference between revisions of "Part:BBa K3329019"

Revision as of 08:56, 27 October 2020

Streptococcal Collagen-like 2 without V domain optimized V2

The wild type of this protein usually contains a V domain which is responsible for stabilizing the downstream folding process of scl2 protein. However, in our project, we designed a SpyTag003-scl2 with V domain-SpyTag003-scl2 without V domain-SpyTag003 structure, in which the V domain in first scl2 protein can stabilize the folding of the other scl2 downstream it. Therefore, the scl2 protein in our project has two different versions from the perspective of V domain. Moreover, due to the different codon preference of P. Pastoris and E. coli, the sequence of scl2 should also be divided into two different types — one for P. Pastoris, and one for E. coli. Together, considering these two factors, we generated scl2 proteins with 4 different types and 2 different versions. The first two don't contain V domain, and the second two contain V domain. Also, the first version (V1) refers to the codon optimization for P. Pastoris, and V2 refers to the codon optimization for E. coli.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 193
Illegal NgoMIV site found at 705
Illegal NgoMIV site found at 906
Illegal AgeI site found at 40
Illegal AgeI site found at 49
Illegal AgeI site found at 121
Illegal AgeI site found at 175
Illegal AgeI site found at 391
1000
INCOMPATIBLE WITH RFC[1000]
Illegal BsaI site found at 592

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K3329019 short</partinfo>
-This sequence code for Streptococcal Collagen-like protein, which is used to modify the bacteria cellulose.Such protein is capable of recreating the texture of leather.
+The wild type of this protein usually contains a V domain which is responsible for stabilizing the downstream folding process of scl2 protein. However, in our project, we designed a SpyTag003-scl2 with V domain-SpyTag003-scl2 without V domain-SpyTag003 structure, in which the V domain in first scl2 protein can stabilize the folding of the other scl2 downstream it. Therefore, the scl2 protein in our project has two different versions from the perspective of V domain. Moreover, due to the different codon preference of P. Pastoris and E. coli, the sequence of scl2 should also be divided into two different types — one for P. Pastoris, and one for E. coli. Together, considering these two factors, we generated scl2 proteins with 4 different types and 2 different versions. The first two don't contain V domain, and the second two contain V domain. Also, the first version (V1) refers to the codon optimization for P. Pastoris, and V2 refers to the codon optimization for E. coli.
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