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Literature summary for 3.4.21.92 extracted from

  • Leodolter, J.; Warweg, J.; Weber-Ban, E.
    The Mycobacterium tuberculosis ClpP1P2 protease interacts asymmetrically with its ATPase partners ClpX and ClpC1 (2015), PLoS ONE, 10, e0125345 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
S61A/Y63V/L83A/Y91V mutations in hydrophobic patch of subunit ClpP1. Complex formation and processing still occurs. The complex containing the mutant is catalytically active Mycobacterium tuberculosis
Y75V/Y95V mutations in hydrophobic patch of subunit ClpP2.Complex formation and processing still occurs. The complex containing the mutant is catalytically inactive Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
 gel filtration, assembled double-ring complex Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPC5 and P9WPC3 P9WPC5 i.e. subunit P1, P9WPC3 i.e. subunit P2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification both subunits ClpP1 and ClpP2 are translated as propeptides. ClpP1 is processed between residues Met7 and Arg8 Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
More the ClpP1P2 double-ring complex can be assembled without activator peptide and ipropeptides are processed in a chaperone-dependent manner Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ClpP1P2
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function Clp chaperones ClpX and ClpC1 require the intact interaction face of subunit ClpP2 to support degradation. Binding results in an asymmetric complex where chaperones only bind to the ClpP2 side of the proteolytic core Mycobacterium tuberculosis