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Literature summary for 3.4.21.53 extracted from

  • Sivertsson, E.M.; Jackson, S.E.; Itzhaki, L.S.
    The AAA+ protease ClpXP can easily degrade a 31 and a 52-knotted protein (2019), Sci. Rep., 9, 2421 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
gene lon, recombinant expression of N-terminally truncated ClpX lacking residues 1-62, i.e. ClpXDELTAN, in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of an N-terminally truncated ClpX lacking residues 1-62, ClpXDELTAN Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 additional information Michaelis-Menten plot of YbeA-ssrA degradation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
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Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally truncated ClpX lacking residues 1-62, from Escherichia coli strain BL21(DE3) Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information N-terminally truncated enzyme ClpXP can easily degrade a deeply 31-knotted and 52-knotted proteins. The degradation depends critically on the location of the degradation tag and the local stability near the tag Escherichia coli ?
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PR65/A-ssrA + H2O ssrA-fusion protein Escherichia coli ?
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ThiS-YbeA + H2O YbeA is a alpha/beta-knot methyltransferase from Escherichia coli and a deeply 31-knotted protein. Knotted fusion protein ThiS-YbeA is degraded by ClpXP. Process modeling, overview Escherichia coli ?
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ThiS-YbeA-ssrA + H2O low activity, process modeling, overview Escherichia coli ?
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UCH-L1-ssrA + H2O ssrA-fusion protein, UCH-L1 is a 52-knotted protein, high activity. In degradation of UCH-L1-ssrA, the degron is located at the C-terminus of the knotted protein. C-terminally tagged UCH-L1-ssrA is not noticeably degraded by ClpXP, while N-terminally tagged ssrA-x-UCH-L1 is degraded by ClpXP. The fact that the C-terminal ssrA-tag is attached directly to beta-strand 6, which is located at the centre of the core beta-sheet structure, may explain the resistance of UCH-L1-ssrA to ClpXP-induced degradation. Mutant UCH-L1-ssrA F162A is stabilised by the mutation, mutant UCH-L1-ssrA F165A is very destabilised Escherichia coli ?
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YbeA-ssrA + H2O YbeA is a alpha/beta-knot methyltransferase from Escherichia coli and a deeply 31-knotted protein. Dimeric YbeA-ssrA (ssrA-tagged fusion protein of YbeA) is degraded rapidly by ClpXP, the rate of ATP-hydrolysis by ClpXP is moderately stimulated during the degradation process. Process modeling, overview Escherichia coli ?
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Synonyms

Synonyms Comment Organism
AAA+ protease
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 Escherichia coli
ClpXP
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP ClpXP is a ATP-dependent protease. ClpXP displays a basal rate of ATP hydrolysis even when not engaged in protein degradation and in the presence of ssrA-tagged substrate PR65/A, although not with UCH-L1-ssrA, the ATPase rate is stimulated Escherichia coli