Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type and mutant enzymes in BW25113 DELTAhslVU::kan cells | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of mixed dodecamers having varied numbers of HslV and T1A subunits, and of a series of HslV dodecamers containing different numbers of active sites showing that HslV with only 6 active sites is sufficient to support full catalytic activity, a further reduction of the number of active sites leads to a proportional decrease in activity. Substrate-mediated stabilization of the HslV-HslU interaction remains unchanged until the number of the active sites is decreased to 6 but is gradually compromised upon further reduction. Deletion of Thr1 causes a dramatic increase in affinity between HslV and HslU | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
lactacystin | in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase | Escherichia coli | |
NLVS | in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
SulA + H2O | Escherichia coli | degradation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes from BW25113 DELTAhslVU::kan cells by nickel affinity chromatography | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP-dependent cleavage of peptide bonds with broad specificity. | model for a proteolytic cycle by HslVU protease, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | degradation | Escherichia coli | ? | - |
? | |
Arc + H2O | degradation | Escherichia coli | ? | - |
? | |
Arc mutant I137A + H2O | monomeric mutant, degradation | Escherichia coli | ? | - |
? | |
additional information | HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV uses the N-terminal threonine as the active site residue. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity, but only 6 active sites are sufficient to support full catalytic activity. Substrate-mediated stabilization of the HslV-HslU interaction | Escherichia coli | ? | - |
? | |
SulA + H2O | degradation | Escherichia coli | ? | - |
? | |
SulA + H2O | recombinant substrate, produced as maltose-binding fusion protein and cleaved by factorXa | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | mathematical models for stochastically assembled HslV dodecamers, overview | Escherichia coli |
oligomer | HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
HslV protease | - |
Escherichia coli |
HslVU ATP-dependent protease | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Escherichia coli |