Difference between revisions of "Part:BBa K3805532"

Revision as of 09:40, 18 October 2021

OmpT signal peptide

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. The protease is expressed in high amounts in E. coli and has a secretory effect. The signal skin sequence can be used to construct a secretory prokaryotic expression vector. 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.

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]

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 <partinfo>BBa_K3805532 short</partinfo>
-Outer membrane protease (OmpT) is a 33.5 kDa aspartyl protease that cleaves at dibasic sites and is thought to function as a defense mechanism for E. coli against cationic antimicrobial peptides secreted by the host immune system.Ompt is one of the four major outer membrane proteases of E. coli, and its protein precursor has a relative molecular mass of 42,000, which is recognized and sheared by the signal skin enzyme during transmembrane, and is 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 outer side of the cell membrane. Since this protease is highly expressed in E. coli and has a secretory effect.
+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.
+The protease is expressed in high amounts in E. coli and has a secretory effect.
+The signal skin sequence can be used to construct a secretory prokaryotic expression vector.
+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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