Activating Compound | Comment | Organism | Structure |
---|---|---|---|
alpha-casein | temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess | Thermus thermophilus | |
Pepsin | temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess | Thermus thermophilus |
Cloned (Comment) | Organism |
---|---|
T.ftsH gene, DNA determination and analysis, expression as His-tagged protein in Escherichia coli | Thermus thermophilus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | strong, complete inhibition at equimolar amounts to ATP | Thermus thermophilus | |
additional information | no inhibition by AMP | Thermus thermophilus | |
o-phenanthroline | chelator for divalent metal ions | Thermus thermophilus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | integral | Thermus thermophilus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | dependent on | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein + H2O | Thermus thermophilus | - |
peptides | - |
? | |
protein + H2O | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
peptides | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q5SI82 | - |
- |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SI82 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli | Thermus thermophilus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
proteolytic degradation of proteins | soluble C-terminal domain harbors the ATPase and protease activity, the N-terminal domain permits the indispensible membrane integration of the enzyme, cleavage of small peptides from the C-terminal side of hydrophobic residues, overview | Thermus thermophilus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
largely unfolded alpha-lactalbumin + H2O | no activity with the native protein, cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates | Thermus thermophilus | peptides | between 10 and 30 kDa, no large intermediates | ? | |
additional information | no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA | Thermus thermophilus | ? | - |
? | |
additional information | no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
protein + H2O | - |
Thermus thermophilus | peptides | - |
? | |
protein + H2O | cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview | Thermus thermophilus | peptides | between 10 and 30 kDa, no large intermediates | ? | |
protein + H2O | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | peptides | - |
? | |
protein + H2O | cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | peptides | between 10 and 30 kDa, no large intermediates | ? | |
unfolded alpha-casein + H2O | - |
Thermus thermophilus | peptides | between 10 and 30 kDa, no large intermediates | ? | |
unfolded alpha-casein + H2O | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | peptides | between 10 and 30 kDa, no large intermediates | ? | |
unfolded pepsin + H2O | cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates | Thermus thermophilus | peptides | between 10 and 30 kDa, no large intermediates | ? | |
unfolded pepsin + H2O | cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | peptides | between 10 and 30 kDa, no large intermediates | ? |
Synonyms | Comment | Organism |
---|---|---|
M41.001 | Merops-ID | Thermus thermophilus |
T.ftsH | - |
Thermus thermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
ATPase activity, recombinant enzyme | Thermus thermophilus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
36 | 70 | 5% of maximal activity at 36°C, 17% of maximal activity at 50°C, 63% of maximal activity at 60°C, and 67% of maximal activity at 70°C | Thermus thermophilus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.65 | - |
ATP | recombinant enzyme | Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Thermus thermophilus | |
CTP | can substitute for ATP by 74% | Thermus thermophilus | |
GTP | can substitute for ATP by 19% | Thermus thermophilus | |
additional information | no activity with TTP, UTP, AMP, and ADP | Thermus thermophilus |