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Literature summary for 3.4.21.92 extracted from

  • Marsee, J.D.; Ridings, A.; Yu, T.; Miller, J.M.
    Mycobacterium tuberculosis ClpC1 N-terminal domain is dispensable for adaptor protein-dependent allosteric regulation (2018), Int. J. Mol. Sci., 19, 3651 .
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
ClpS adaptor protein ClpS is inhibitory to ClpC1. the unfolding rate of substrates shows a a nearly three-fold for conditions lacking ClpS relative to conditions with ClpS in excess Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPC9
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Mycobacterium tuberculosis H37Rv P9WPC9
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-

Synonyms

Synonyms Comment Organism
ClpC1
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 Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function ClpC1-catalyzed unfolding of an SsrA-tagged protein is negatively impacted by association with the ClpS adaptor protein. ClpS-dependent inhibition of ClpC1-catalyzed SsrA-dependent protein unfolding does not require the ClpC1 N-terminal domain but instead requires the presence of an interaction surface located in the ClpC1 middle domain Mycobacterium tuberculosis