EC Number   |
Subunits |
Reference |
|---|
   3.4.21.92 | More |
ClpP subunits (MW 21500 Da) are arranged in two hexagonal rings directly superimposed on each other, ClpA (subunit 83000) and ClpP do not associate in absence of ATP |
29867 |
| 3.4.21.92 | More |
ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein |
-, 29858, 29865, 29866 |
| 3.4.21.92 | More |
effective degradation by enzyme requires an intact complex with N-terminal domains of ClpA chaperone protein to ensure the unfolding of substrates and targeting of unfolded substrates to the protease |
669410 |
| 3.4.21.92 | More |
enzyme consists of two components: ClpP and ClpA or ClpX |
-, 29857, 29858, 29860, 29862, 29865, 29866, 29868 |
| 3.4.21.92 | More |
tetradecamer, sedimentation velocity analytical ultracentrifugation |
718406 |
| 3.4.21.92 | More |
the ClpP1P2 double-ring complex can be assembled without activator peptide and ipropeptides are processed in a chaperone-dependent manner |
755086 |
| 3.4.21.92 | More |
the enzyme is a complex consisting of two components I and II, that can be separated from each other |
29861 |
| 3.4.21.92 | More |
there exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP |
669324 |
| 3.4.21.92 | More |
Two soluble Clp proteolytic cores consisting of distinct pairs of ClpP/R paralogs, ClpP1/P2 and ClpP3/R exist in cyanobacteria. Each proteolytic core associates with a different HSP100 partner, ClpX with ClpP1/P2 and ClpC with ClpP3/R, ClpC with two ClpS adaptors. |
683643 |
| 3.4.21.92 | multimer |
n * 230000, n * 180000, ClpP1, ClpP3, clpP4, ClpP5, clpP6, clpR1, clpR2, ClpR3, cClR4, ClpS1 |
683977 |
