Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Max Schelski
Date created: 2013-09-21 11:00:00
Date modified: 2015-05-08 01:09:02
E. coli sspB[Core]
| Types | DnaRegion |
| Roles | Protein_Domain polypeptide_domain |
| Sequences | BBa_K1075008_sequence (Version 1) |
Description
EcsspB itself regulates the degradation of ssrA tagged proteins through the ClpXP protease in procaryotes. In engineered systems it is used to induce degradation of specifically ssrA tagged proteins.This construct is part of the split system of E. Coli sspB (EcsspB) which was used in fusion with FKBP and FRB to induce the activity of sspB and therefore degradation of proteins with Rapamycins. [1]
EcsspB can be functionally divided in three parts: [2]
-the N terminal Core domain (113 AA)
-the C terminal XB peptide (25 AA)
-and a 'flexible linker' in between the first parts (28 AA)
We used the same domain structure as is used within the Rapamycin inducable split system. [1]
While the Core domain is responsible for dimerization of sspB and binding of ssrA the XB peptide binds the protease ClpXP. The flexible linker is called flexible because it was found, that an increase or reduction in size or amino acid composition does not influence the function of sspB as much as it would in the other domains. [3]
For our project we needed the sspB split system to engineer a light inducable sspB.