Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | ClpP3/R complex stimulates the steady-state ATPase activity of ClpC | Synechococcus elongatus |
Cloned (Comment) | Organism |
---|---|
clpP3 and clpR genes cloned into the pACYC Duet vector for co-expression in Escherichia coli BL21-STAR cells | Synechococcus elongatus |
Protein Variants | Comment | Organism |
---|---|---|
S101A | mutation of the active site Ser-101 in ClpP3 inactivates the entire ClpCP3/R protease, the mutation has no effect on the formation of the recombinant ClpP3/R core complex of 270 kDa. The mutated ClpP3/R complex stimulates the steady-state ATPase activity of ClpC to the same extent as wild-type ClpP3/R. The mutated ClpP3/R core fails to degrade the alpha-casein nor the more sensitive FITC-casein | Synechococcus elongatus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
270000 | - |
native-PAGE | Synechococcus elongatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechococcus elongatus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
ClpP3/R complex purified on Ni2+ affinity column and by gel filtration, purification of ClpC and ClpS1 | Synechococcus elongatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | is completely degraded by ClpC and ClpP3/R within 20 min | Synechococcus elongatus | ? | - |
? | |
FITC-casein + H2O | neither ClpC nor ClpP3/R alone degrade FITC-casein but they do when added together. No proteolytic activity when ClpP3 alone is combined with ClpC | Synechococcus elongatus | ? | - |
? | |
FR-GFP + H2O | ClpCP3/R with ClpS1 take over 20 min to completely degrade FR-GFP, whereas the ClpAP protease degrades all FR-GFP within 2 min | Synechococcus elongatus | ? | - |
? | |
additional information | ClpR subunit is proteolytically inactive, thus ClpR subunit does not contribute to the proteolytic activity of the ClpP3/R core. Inclusion of ClpR is not rate-limiting for the ClpCP3/R protease. ClpC is not affected by auto-degradation as is ClpA. ClpS1 alters the substrate specificity of the ClpCP3/R protease | Synechococcus elongatus | ? | - |
? | |
N-succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O | throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation | Synechococcus elongatus | N-succinyl-Ile-Ile-Trp + 7-amino-4-methylcoumarin | - |
? | |
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation | Synechococcus elongatus | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
N-succinyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O | throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation | Synechococcus elongatus | N-succinyl-Val-Lys-Met + 7-amino-4-methylcoumarin | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | ClpP3/R complex, SDS-PAGE | Synechococcus elongatus |
Synonyms | Comment | Organism |
---|---|---|
Clp protease | - |
Synechococcus elongatus |
ClpA | - |
Synechococcus elongatus |
ClpC | - |
Synechococcus elongatus |
ClpCP3/R protease | - |
Synechococcus elongatus |
ClpP | - |
Synechococcus elongatus |
ClpP3 | - |
Synechococcus elongatus |
ClpP3/R complex | - |
Synechococcus elongatus |
ClpR | - |
Synechococcus elongatus |
ClpS1 | - |
Synechococcus elongatus |