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UniProt functional annotation for P9WPC5 | ||
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| UniProt code: P9WPC5. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:23314154}. |
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| Catalytic activity: | |
Reaction=Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444}; |
| Subunit: | |
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Forms a complex with ClpP2 and ClpX. {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:17242518, ECO:0000269|PubMed:23314154}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. |
| Similarity: | |
Belongs to the peptidase S14 family. {ECO:0000255|HAMAP- Rule:MF_00444}. |
Annotations taken from UniProtKB at the EBI.