Protein Variants | Comment | Organism |
---|---|---|
G90P | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview, the mutant shows 41% reduced ATP hydrolysis activity compared to wild-type HslU | Escherichia coli |
G93A | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
G93P | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
V92A | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
V92I | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
V92S | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
Y91A | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
Y91F | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
Y91S | mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber | ? | - |
? | |
SulA + H2O | Escherichia coli | specific substrate degradation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | the structural features of the GYVG motif increase degrading activity | Escherichia coli | ? | - |
? | |
ATP + H2O | - |
Escherichia coli | ADP + phosphate | - |
? | |
additional information | the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber | Escherichia coli | ? | - |
? | |
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O | - |
Escherichia coli | N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin | - |
? | |
SulA + H2O | specific substrate degradation | Escherichia coli | ? | - |
? | |
SulA-maltose binding protein-fusion protein + H2O | recombinant substrate, specific substrate degradation requires the flexibility provided by glycine residues and aromatic ring structures of the first 91 amino acids | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | HslV, the proteolytic active sites are sequestered in the inner chamber of HslV | Escherichia coli |
hexamer | HslU | Escherichia coli |
More | structure analysis using crystal structure PDB code 1G4A, the GYVG motif is essential for enzyme complex activity, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
HslU ATPase | - |
Escherichia coli |
HslUV | - |
Escherichia coli |
HslV peptidase | - |
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, HslU, ATP cleavage involves the pore motif GYVG | Escherichia coli |