| Types | DnaRegion
|
| Roles | Coding
CDS
|
| Sequences | BBa_K365004_sequence (Version 1)
|
Description
In wild type E. coli, ClpX forms a ring of hexamer and binds to a double heptamer of ClpP. ClpX recognizes a specific C-terminal degradation tag called SsrA and starts to unfold the tagged protein. The denatured polypeptide is translocated into the ClpP subunit, which breaks peptide bonds. The N terminal end of ClpX contains a domain which is responsible for interaction with its natural adaptator protein (SspB) that we would avoid. As this N-terminal domain is also partially responsible for ClpX subunits complexation into an hexamer, fusing three C-terminal end of ClpX together with appropriate linkers increases the stability of the system (T. Baker et al.) in the absence of this N-terminal domain.
Notes
We deleted 2 EcoRI sites and 2 Age1 sites by directed mutagenis at positions 522 and 967, and 183 and 921 respectively. This biobrick has standard RFC-25.
Source
Genomic sequence from E.coli.
