Difference between revisions of "Part:BBa K233307"

 
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<partinfo>BBa_K233307 short</partinfo>
 
<partinfo>BBa_K233307 short</partinfo>
  
The twin arginine translocation (Tat)4 pathway serves to transport folded proteins across energy-transducing membranes
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The twin arginine translocation (Tat)pathway serves to transport folded proteins across energy-transducing membranes in archaea, bacteria, and the chloroplasts of plants . In bacteria, polypeptides exported via the Tat pathway include redox enzymes, virulence factors, periplasmic ligandbinding proteins, and enzymes involved in cell envelope biogenesis . Only proteins that can attain a folded state in the cytoplasm are competent for export via Tat . Translocation across the membrane is initiated by the interaction of the signal peptide with the Tat machinery, which in Escherichia coli consists of the membrane proteins TatABC. The amino-terminal (n-) region contains the Tat consensus motif (S/T)RRXFLK, which includes the signature twin arginine dipeptide.
in archaea, bacteria, and the chloroplasts of plants (1–4). In bacteria, polypeptides exported via the Tat pathway
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include redox enzymes, virulence factors, periplasmic ligandbinding proteins, and enzymes involved in cell envelope biogenesis
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(5). Only proteins that can attain a folded state in the cytoplasm are competent for export via Tat (2, 6). Translocation
+
across the membrane is initiated by the interaction of the signal peptide with the Tat machinery, which in Escherichia coli
+
consists of the membrane proteins TatABC. The amino-terminal (n-) region contains the Tat consensus motif (S/T)RRXFLK, which includes the signature twin arginine
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dipeptide.
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Latest revision as of 09:36, 18 October 2009

TorA- This part is a export tag that utilizes the Twin Arginine Transport pathway(TAT)

The twin arginine translocation (Tat)pathway serves to transport folded proteins across energy-transducing membranes in archaea, bacteria, and the chloroplasts of plants . In bacteria, polypeptides exported via the Tat pathway include redox enzymes, virulence factors, periplasmic ligandbinding proteins, and enzymes involved in cell envelope biogenesis . Only proteins that can attain a folded state in the cytoplasm are competent for export via Tat . Translocation across the membrane is initiated by the interaction of the signal peptide with the Tat machinery, which in Escherichia coli consists of the membrane proteins TatABC. The amino-terminal (n-) region contains the Tat consensus motif (S/T)RRXFLK, which includes the signature twin arginine dipeptide.

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]