Part:BBa_K3121003
RBS_Cpn10+RBS_Cpn60
We identified the Cpn 10/60 chaperone system (isolated from Oleispira antarctica). The chaperonin 10/60 is homologous to the GroEL/ES chaperonin system in E. coli. Essentially, these are active assistants for protein folding processes. The advantage here is that Cpn 10/60 is a cold-active component, i.e., unlike the mesophilic chaperone systems which are highly inefficient at lower temperatures, these cold-active entities perform optimally at cold temperatures. The Cpn 10/60 which predominantly retains a double ring form at mesophilic temperature ranges (excess of 24℃), shifts to a single ring form at lower temperatures (4-10℃). This is especially relevant since single ring conformations are more energetically efficient.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1211
Illegal BamHI site found at 1277 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 70
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