Cloned (Comment) | Organism |
---|---|
genes clpY, co-expression of ClpQ and ClpY mutants in AC3112 cells. Co-expression of ClpY with HA-tagged SulA and mutant SulA M89I, RcsA, RpoH, and TraJ molecules in the yeast two-hybrid system, expression of recombinant ClpYQ mutants | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
A188S | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview | Escherichia coli |
E193L/E194L | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview | Escherichia coli |
E61C | clpQ mutant | Escherichia coli |
I186N | clpY mutant, the mutant does not interact with SulA compared to the wild-type ClpY | Escherichia coli |
L199Q | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview. SulA accumulates in the bacterial cells that express ClpY | Escherichia coli |
M187I | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview | Escherichia coli |
additional information | construction of truncation mutants lacking the substrate binding residues 137-209 of ClpY | Escherichia coli |
N141L/N142L | the ClpY loop 1 mutant is defective in complete degradation of SulA | Escherichia coli |
N205K | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview | Escherichia coli |
Q148L/Q149L/Q150L | the ClpY loop 1 mutant shows altered substrate recognition and binding, but shows normal activity similar to that of the wild-type ClpY | Escherichia coli |
Q198L/Q200L | clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview | ? | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview | Escherichia coli | ? | - |
? | |
additional information | ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. The ATP-dependent proteolysis is mediated by substrate recognition in the ClpYQ complex | Escherichia coli | ? | - |
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Subunits | Comment | Organism |
---|---|---|
More | ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. ClpY has three domains, N, I, and C, and these domains are discrete and exhibit different binding preferences | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ClpYQ | - |
Escherichia coli |
ClpYQ protease | - |
Escherichia coli |
HslUV | - |
Escherichia coli |
HslUV protease | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Escherichia coli |