Difference between revisions of "Part:BBa K1714005"

Revision as of 23:27, 18 September 2015

pBad/araC-RBS B0034-Ag43 thanatin 2mer as alpha domain-double terminator

Ag43 is a kind of outer membrane protein that is composed of some domains. First one is signal peptide that transport Ag43 to outer membrane. After transportation, the signal peptide is cleaved and left at inner membrane. Second one is alpha domain that has connection peptide to another Ag43 alpha domain. Last one is beta domain that has beta barrel structure to let the barrel there. Due to the function of a part of beta domain, called auto-chaperon domain, alpha domain is let outside of the membrane. This part has thanatin, a kind of antimicrobial peptide 2mer as alpha domain. This thanatin has Asp(Aspartic acid) as the last residue. So if thanatin domain is digested by Asp-N endoproteinase (NEB), this part secrets feature of thanatins, losing toxicity.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 1205
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 1540
Illegal BamHI site found at 1144
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 1822
Illegal NgoMIV site found at 2332
Illegal NgoMIV site found at 2353
Illegal AgeI site found at 979
Illegal AgeI site found at 1413
Illegal AgeI site found at 1485
Illegal AgeI site found at 2092
Illegal AgeI site found at 2506
Illegal AgeI site found at 2748
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI site found at 961

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 <partinfo>BBa_K1714005 short</partinfo>
-Ag43 is a kind of outer membrane protein that is composed of some domains. First one is signal peptide that transport Ag43 to outer membrane. After transportation, the signal peptide is cleaved and left at inner membrane. Second one is alpha domain that has connection peptide to another Ag43 alpha domain. Last one is beta domain that has beta barrel structure to let the barrel there. Due to the function of a part of beta domain, called auto-chaperon domain, alpha domain is let outside of the membrane. This part has thanatin, a kind of antimicrobial peptide 2mer as alpha domain. This thanatin has Asp as the last residue. So if thanatin domain is digested by Asp-N endoproteinase (NEB), this part secrets thanatins.
+Ag43 is a kind of outer membrane protein that is composed of some domains. First one is signal peptide that transport Ag43 to outer membrane. After transportation, the signal peptide is cleaved and left at inner membrane. Second one is alpha domain that has connection peptide to another Ag43 alpha domain. Last one is beta domain that has beta barrel structure to let the barrel there. Due to the function of a part of beta domain, called auto-chaperon domain, alpha domain is let outside of the membrane. This part has thanatin, a kind of antimicrobial peptide 2mer as alpha domain. This thanatin has Asp(Aspartic acid) as the last residue. So if thanatin domain is digested by Asp-N endoproteinase (NEB), this part secrets feature of thanatins, losing toxicity.
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