Difference between revisions of "Part:BBa K116601"
 
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Metadata:  
 
Metadata:  
  
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Group: City of London UK 2021
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*'''Group''': City of London UK 2021
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*'''Author''': Julian Chen
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Author: Julian Chen
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*'''Summary''': Added information collated from existing scientific studies  
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Summary: Added information collated from existing scientific studies  
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Plays a role in the quality control of integral membrane proteins. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements.  
 
Plays a role in the quality control of integral membrane proteins. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements.  
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Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.
 
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It degrades ceratin membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA, as well as cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein.
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Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.
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As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS). It transports the toxic C-terminal region of CdiA from E.coli strain 536, E.cloacae strain ATCC 13047 and of Y.pestis strain A across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins.
 
<ref>'Uniprot. https://www.uniprot.org/uniprot/P0AAI3</ref>
 
<ref>'Uniprot. https://www.uniprot.org/uniprot/P0AAI3</ref>
  
  
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===Usage and Biology===
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===Sequence and Features===
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K116601 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K116601 SequenceAndFeatures</partinfo>
  
  
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===References===
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===Functional Parameters===
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<partinfo>BBa_K116601 parameters</partinfo>
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Latest revision as of 16:51, 1 October 2021


HtlB (ftsH) coding region from E. coli

The HtlB (ftsH) coding region from E. coli. It can be used to degrade many different proteins.

Information contributed by City of London UK (2021)

Part information is collated here to help future users of the BioBrick registry.

Metadata:

  • Group: City of London UK 2021
  • Author: Julian Chen
  • Summary: Added information collated from existing scientific studies


Plays a role in the quality control of integral membrane proteins. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements.

It degrades ceratin membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA, as well as cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA. As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS). It transports the toxic C-terminal region of CdiA from E.coli strain 536, E.cloacae strain ATCC 13047 and of Y.pestis strain A across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins. [1]


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 219
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 586
    Illegal AgeI site found at 1459
  • 1000
    COMPATIBLE WITH RFC[1000]


References

  1. ↑ 'Uniprot. https://www.uniprot.org/uniprot/P0AAI3