Function
proteolytic subunit
ClpXP is an ATP-dependent protease of the mitochondrial matrix. Hexameric rings of the AAA+ unfoldase ClpX recognise substrates, unfold them and thread them into the barrel formed by two heptameric rings of the serine peptidase ClpP, where they are degraded. ClpXP contributes to matrix protein quality control and to the mitochondrial unfolded protein response.
FlyBase groups realized by this module: CLPXP (FBgg0002017). Participants were generated from the FlyBase gene-group membership and mapped to UniProtKB by projects/FLYBASE_GENE_GROUPS/generate_modules.py from module_specs/dmel_mitochondrial_clpxp.yaml. Member genes with a gene review in this repository: ClpP, ClpX.
All recommended fields populated.
✗ none found
No MODULE:dmel_mitochondrial_clpxp deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
1 gene-function check(s) reflected in core functions · 0 conflict(s) · 0 evidence or coverage gap(s) (1 comparison(s))
Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.
| Annoton | Participant | Function | Assessment |
|---|---|---|---|
| dmel_mitochondrial_clpxp_clpp_clpp | ClpP UniProtKB:Q9VKY3 Gene |
serine-type endopeptidase activity GO:0004252 |
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass). |
2 complete review(s) · 1 with deep research · 0 missing review · 1 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| ClpP Q9VKY3 | ✓ | ✓ | ✓ |
| ClpX A0A0B4LID7 | ✓ | ✓ | ✗ |
ATP-dependent matrix protease made of the ClpX unfoldase and the ClpP peptidase.
proteolytic subunit
ATP-dependent unfoldase subunit