Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of deletion mutants DELTA175-209linker, DELTA175-209GG, and DELTA108-243GG | Escherichia coli |
Y91A | site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows no remaining activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity | Escherichia coli |
Y91F | site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows reduced activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state kinetics of wild-type and point mutant as well as deletion mutant enzymes with Arc substrates and ATP, overview | Escherichia coli | |
0.02 | - |
Arc-st11-ssrA | wild-type HslU, pH 7.6, 37°C | Escherichia coli | |
0.026 | - |
Arc-st11-ssrA | HslU mutant Y91F, pH 7.6, 37°C | Escherichia coli | |
0.125 | - |
Arc-st11-ssrA | deletion mutant DELTA175-209linker, pH 7.6, 37°C | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Arc repressor + H2O | interaction of Arc substrates with HslU variants bearing mutations in the GYVG pore loop or the I domain, overview. N-terminal residues of Arc initially interact with the GYVG loop in the axial pore of HslU, while other portions of Arc contact disordered I-domain loops, residues 175-209, that project into the substrate-binding funnel above the pore | Escherichia coli | ? | - |
? | |
Arc-st11-ssrA + H2O | wild-type HslU binds this fluorescent substrate with an average affinity, whereas the Y91A mutant variant shows no detectable binding. Tyr91 side chain plays an important role in allowing HslU to bind Arc-st11-ssrA | Escherichia coli | ? | - |
? | |
additional information | substrates are typically targeted to specific AAA+ proteases by peptide sequences. In the AAA+ HslUV protease, substrates are bound and unfolded by a ring hexamer of HslU, before translocation through an axial pore and into the HslV degradation chamber. The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine | Escherichia coli | ? | - |
? | |
SulA + H2O | as MBP-SulA fusion protein | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AAA+ HslUV protease | - |
Escherichia coli |
HslUV | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on. The intermediate domain of HslU is required for robust ATP hydrolysis, ATP hydrolysis activities of wild-type and mutant enzymes, overview | Escherichia coli | |
additional information | HslU does not hydrolyze ATPgammaS, an ATP analogue | Escherichia coli |