Recombinant Vibrio fischeri Protease HtpX (htpX)
Description
Protein Overview
HtpX belongs to the heat shock protein family and functions as a zinc-dependent endoprotease. In V. fischeri, it is recombinantly expressed with a His₆ tag for purification . Key features include:
Sequence Analysis
The amino acid sequences of HtpX from V. fischeri strains MJ11 and ES114 show high similarity, with minor differences:
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Key Motifs:
Inferred Roles in Protein Quality Control
While V. fischeri HtpX has not been directly studied, its E. coli homolog participates in:
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Membrane Protein Degradation: Cleaves SecY and other misfolded proteins .
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Stress Response: Activated during cellular stress (e.g., heat shock) .
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Zinc Dependency: Requires Zn²⁺ for catalytic activity, with self-degradation observed in its absence .
Experimental Challenges
Recombinant HtpX purification requires careful handling due to:
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Self-Degradation: Spontaneous cleavage upon cell disruption or membrane solubilization .
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Refolding Requirements: Purification under denaturing conditions followed by refolding with zinc supplementation .
Research Gaps
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Functional Studies: No published data on V. fischeri HtpX's role in symbiosis or host interactions.
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Regulatory Pathways: Unlike E. coli, its interaction with FtsH or other proteases remains unexplored.
Comparative Analysis with E. coli HtpX
Product Specs
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The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its inclusion.
Target Background
KEGG: vfm:VFMJ11_1232
