Difference between revisions of "Part:BBa K4905019"

 
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The E.coli K-12 strain possesses a protein, called the outer membrane protein F (Ompf). The precursor of this protein contains a signaling peptide 22 amino acids in length, which is the Ompf signaling sequence [1]. This sequence is used for translocating proteins from the cytoplasm to the periplasm [2]. For this reason, the Ompf sequence can be fused to other proteins for the secretion into the periplasm [3]
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The <i>E.coli</i> K-12 strain possesses a protein, called the outer membrane protein F (Ompf). The precursor of this protein contains a signaling peptide 22 amino acids in length, which is the Ompf signaling sequence<sup>[1]</sup>. This sequence is used for translocating proteins from the cytoplasm to the periplasm<sup>[2]</sup>. For this reason, the Ompf sequence can be fused to other proteins for the secretion into the periplasm<sup>[3]</sup>.
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References
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[1]:Inokuchi K, Mutoh N, Matsuyama S, Mizushima S (1982) Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12. Nucleic Acids Res 10:6957-6968
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[2]:Vlasuk GP, Inouye S, Ito H, Itakura K, Inouye M (1983) Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. J Biol Chem 258:7141-7148
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<span class='h3bb'>Sequence and Features</span>
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[3]: Yamamoto, T, Okawa N.,Endo T., and Kaji A. (1991) Expression of chimeric ras protein with OmpF signal peptide in Escherichia coli: localization of OmpF fusion protein in the inner membrane. Appl Microbiol BiotechnoZ 35:615-621
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<h1>References</h1>
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[1] Inokuchi K, Mutoh N, Matsuyama S, Mizushima S (1982) Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12. Nucleic Acids Res 10:6957-6968
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[2] Vlasuk GP, Inouye S, Ito H, Itakura K, Inouye M (1983) Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. J Biol Chem 258:7141-7148
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[3] Yamamoto, T, Okawa N.,Endo T., and Kaji A. (1991) Expression of chimeric ras protein with OmpF signal peptide in Escherichia coli: localization of OmpF fusion protein in the inner membrane. Appl Microbiol BiotechnoZ 35:615-621
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===Usage and Biology===
 
===Usage and Biology===
  
 
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Revision as of 09:30, 26 September 2023


The Ompf sequence is a signaling peptide allowing for translocation of a protein to the periplasm

The E.coli K-12 strain possesses a protein, called the outer membrane protein F (Ompf). The precursor of this protein contains a signaling peptide 22 amino acids in length, which is the Ompf signaling sequence[1]. This sequence is used for translocating proteins from the cytoplasm to the periplasm[2]. For this reason, the Ompf sequence can be fused to other proteins for the secretion into the periplasm[3].

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]

References

[1] Inokuchi K, Mutoh N, Matsuyama S, Mizushima S (1982) Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12. Nucleic Acids Res 10:6957-6968 [2] Vlasuk GP, Inouye S, Ito H, Itakura K, Inouye M (1983) Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. J Biol Chem 258:7141-7148 [3] Yamamoto, T, Okawa N.,Endo T., and Kaji A. (1991) Expression of chimeric ras protein with OmpF signal peptide in Escherichia coli: localization of OmpF fusion protein in the inner membrane. Appl Microbiol BiotechnoZ 35:615-621