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Literature summary extracted from
- Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement (2015), J. Biol. Chem., 290, 9789-9800.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.4.10 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Thermus thermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.6.4.10 | E271Q/R576C/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | E271Q/R576C/E668Q/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | K204A/T205A/R576C/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | K204A/T205A/R576C/K601A/K602A/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | additional information | preparation of ordered heterohexamers of ClpB from Thermus thermophilus, in which two subunits having different mutations were cross-linked to each other and arranged alternately. ATPase activities of ordered heterohexamers with varyying mutations in the Walker A and B motifs, or the Arg-finger, of the two D domains, overview | Thermus thermophilus |
| 3.6.4.10 | Q184C/A390C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/A390C/E668Q | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/A390C/K601A/K602A | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/A390C/R747A | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/E271Q/A390C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/E271Q/A390C/E668Q | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/K204A/T205A/A390C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/K204A/T205A/A390C/K601A/K602A | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | Q184C/R322A/A390C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | R322A/R576C/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | R576C/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | R576C/E668Q/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | R576C/K601A/K602A/A821C | site-directed mutagenesis | Thermus thermophilus |
| 3.6.4.10 | R576C/R747A/A821C | site-directed mutagenesis | Thermus thermophilus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.4.10 | Mg2+ | required | Thermus thermophilus |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.10 | ATP + H2O | Thermus thermophilus | - |
ADP + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.4.10 | Thermus thermophilus | Q9RA63 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.4.10 | recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) | Thermus thermophilus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.4.10 | ATP + H2O | - |
Thermus thermophilus | ADP + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.4.10 | heterohexamer | a ring-shaped ClpB hexamer | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.4.10 | AAA+ chaperone ClpB | - |
Thermus thermophilus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.10 | 55 | - |
protein aggregate reactivation assay at | Thermus thermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.4.10 | 7.5 | - |
assay at | Thermus thermophilus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.4.10 | malfunction | intercalation of ATPase defective subunits into the hexamer every other subunit hampers its ATPase and disaggregation activities | Thermus thermophilus |
| 3.6.4.10 | additional information | the ATPase cycle of ClpB proceeded as follows: (i) the 12 AAA+ modules randomly bound ATP, (ii) the binding of four or more ATP to one AAA+ ring is sensed by a conserved Arg residue and converted another AAA+ ring into the ATPase-active form, and (iii) ATP hydrolysis occurred cooperatively in each ring. Protein disaggregation activities of wild-type and cross-linked enzyme TClpB in cooperation with TDnaK system | Thermus thermophilus |
| 3.6.4.10 | physiological function | the ClpB hexamer hydrolyzes ATP and reactivates protein aggregates. ClpB cooperatively hydrolyzes ATP, and this cooperativity is crucial for protein disaggregation. Subunit D1 and D2 dimers have the essential properties of TClpB, evaluation of intersubunit cooperativity, overview | Thermus thermophilus |
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