Part:BBa_K4863005
T7_hpCA_Slp
alpha type carbonic anhydrase fused with s-layer protein via a flexible linker for surface display of hpCA on the cell surface of Synechocystis PCC6803. This yields a cell completely covered in the fusion protein. Surface display maximizes hpCA's binding to substrate and ensures its stability.
Usage and Biology
The fusion of a protein to the Slp N-terminus has proved to be an effective system for the functional surface display of cyanobacteria. For the project of this year, we displayed α-carbonic anhydrase hpCA on the Synechocystis PCC6803 cell surface with the fusion with Slp on the cell surface for the production of calcium carbonate precipitates.
hpCA is a metalloenzymes responsible for catalyzing the interconversion of carbon dioxide (CO2) to bicarbonate ions (HCO3−). It is an α-carbonic anhydrase isolated from the bacterium Helicobacter pylori 26695, codon optimized for expression in E. Coli BL21(DE3). Slp forms the paracrystalline S-layer by forming a regular lattice through an entropy-driven process. It has an undefined signal peptide at the C-terminus.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 443
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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