Difference between revisions of "Part:BBa K3805532"

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<partinfo>BBa_K3805532 short</partinfo>
 
<partinfo>BBa_K3805532 short</partinfo>
  
OmpT is one of the four major outer membrane proteases of E. coli. Its protein precursor has a relative molecular mass of 42,000, which is recognized and sheared by the signal skin enzyme during transmembrane, removing 19 amino acid residues from its amino terminus, and processed into a mature outer membrane protease with a relative molecular mass of 40,000, which is secreted into the peripheral lumen of the cell and localized on the outside of the cell membrane.
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As the signal peptide of one of the major outer membrane proteins ompT, it has the potential to induce the secretion of certain proteins. It originally has 19 amino acids and two additional amino residues was added to the C-terminus for better cleavage of the signal peptide.
The protease is expressed in high amounts in E. coli and has a secretory effect.
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The signal skin sequence can be used to construct a secretory prokaryotic expression vector.
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The OmpT signal skin contains 19 amino acid residues, and two additional amino acid residues were added to the C-terminus of the signal peptide in consideration of the shear recognition amino acid sequence.
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Latest revision as of 10:23, 21 October 2021


OmpT signal peptide

As the signal peptide of one of the major outer membrane proteins ompT, it has the potential to induce the secretion of certain proteins. It originally has 19 amino acids and two additional amino residues was added to the C-terminus for better cleavage of the signal peptide.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]