Function
Processes
Locations
Small ATP-independent chaperone-like protein shown in vitro to prevent PurK aggregation and promote refolding of a model client.
A draft single-protein module for the small E. coli YrhB protein, which has been reported to prevent heat-induced PurK aggregation and support refolding of a model client without ATP. The purified K-12 and BL21(DE3) proteins are identical, but the physiological client set and whether this is a native chaperone function rather than an overexpression-associated moonlighting behavior remain unresolved.
No adjacent cognate toxin gene exists in E. coli K-12, so this module does not include the predicted Imm35 peptidase-inhibitor/polymorphic-toxin immunity activity.
All recommended fields populated.
✗ none found
No MODULE:yrhb_chaperone_like_refolding 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 |
|---|---|---|---|
| yrhb_chaperone_like_activity | E. coli YrhB UniProtKB:P46857 Gene |
protein folding chaperone GO:0044183 |
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass). |
1 complete review(s) · 1 with deep research · 0 missing review · 0 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| yrhB P46857 | ✓ | ✓ | ✓ |
Small ATP-independent chaperone-like protein shown in vitro to prevent PurK aggregation and promote refolding of a model client.