Bacterial GroEL/GroES chaperonin folding

A bacterial cytosolic chaperonin module in which GroEL double rings, capped by GroES, use cycles of ATP binding and hydrolysis to encapsulate non-native polypeptides and release folded clients. The HOCl-activated chaperedoxin CnoX can plug into this system by protecting oxidizing GroEL clients through holdase binding and reversible mixed-disulfide formation, then dissociating when GroES binds.

MODULE:bacterial_groel_groes_chaperonin_foldingDRAFTCONCRETEBiological Processmodules/bacterial_groel_groes_chaperonin_folding.yaml
ATP-dependent protein folding chaperoneGO:0140662 protein refoldingGO:0042026
GO:0140662
ATP-dependent protein folding chaperone
Defines the ATP-dependent GroEL/GroES chaperonin folding activity.
GO:1990220
GroEL-GroES complex
Defines the bacterial chaperonin complex.
file:genes/ECOLI/GroEL/GroEL-ai-review.yaml
ECOLI GroEL gene review
The completed E. coli GroEL review grounds GroEL as the ATP-dependent protein-folding chaperone subunit of the GroEL/GroES complex.
file:genes/ECOLI/groS/groS-ai-review.yaml
ECOLI groS gene review
The completed E. coli groS review grounds GroES as the co-chaperonin lid of the GroEL/GroES complex.
file:genes/ECOLI/CnoX/CnoX-ai-review.yaml
ECOLI CnoX gene review
The completed E. coli CnoX review grounds CnoX as an HOCl-activated chaperedoxin and GroEL-binding redox-quality-control factor.
PMID:7935796
Residues in chaperonin GroEL required for polypeptide binding and release.
Identifies GroEL residues used for polypeptide and GroES binding and ATP-driven client release.
PMID:9285585
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Establishes the functional asymmetric GroEL/GroES architecture that encapsulates folding clients.
PMID:29754824
CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation.
Establishes CnoX as an HOCl-activated holdase/redox protector for clients of the major DnaK and GroEL folding systems.
PMID:36764293
A molecular device for the redox quality control of GroEL/ES substrates.
Establishes the stable CnoX-GroEL complex, mixed-disulfide capture of GroEL clients, and GroES-triggered release of CnoX.

The completed GroEL and groS ECOLI reviews cover the core chaperonin cage. CnoX is modeled as an optional HOCl-activated stress plugin rather than as a constitutive part of the GroEL/GroES foldase.

3Nodes
2Parts
0Variant Sets
0Variants
3Annotons
0Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:bacterial_groel_groes_chaperonin_folding deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Function consistency and core coverage

1 gene-function check(s) reflected in core functions · 0 conflict(s) · 1 evidence or coverage gap(s) (3 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.

AnnotonParticipantFunctionAssessment
groel_groes_chaperonin PROTEIN_COMPLEX
Gene 		ATP-dependent protein folding chaperone
GO:0140662 		Participant Unchecked
No direct UniProt participant to compare. Abstract selectors and complex-wide activities cannot be inferred from donor or subunit gene reviews.
cnox_holdase_chaperedoxin E. coli CnoX
UniProtKB:P77395
Gene 		holdase chaperone activity
No function ID 		No Function Id
A gene review exists, but this function lacks a GO identifier. Free-text chemistry is not automatically compared.
cnox_groel_binding E. coli CnoX
UniProtKB:P77395
Gene 		protein-folding chaperone binding
GO:0051087 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).

Gene-review completeness (3/3 grounded genes reviewed)

3 complete review(s) · 2 with deep research · 0 missing review · 1 reviewed but lacking deep research

Gene Review Complete Deep research
CnoX P77395 ✓ ✓ ✓
GroEL P0A6F5 ✓ ✓ ✓
groS P0A6F9 ✓ ✓ ✗

Details

Context
bacteriaNCBITaxon:2
Bacterial GroEL/GroES chaperonin foldingBiological Processbacterial_groel_groes_chaperonin_folding
ATP-dependent protein folding chaperoneGO:0140662 protein refoldingGO:0042026
Context
bacteriaNCBITaxon:2
Part 1: ATP-dependent GroEL/GroES folding cage
GroEL/GroES ATP-dependent folding cageBiological Processgroel_groes_folding_cage

Annotons

GroEL/GroES chaperonin
groel_groes_chaperonin
Participant: Protein Complex: E. coli GroEL-GroES complex
Protein Complex:
E. coli GroEL-GroES complexGO:1990220
Active units:
GroEL chaperonin ring subunit
Participant: Gene Product: E. coli GroEL
Gene Product:
E. coli GroELUniProtKB:P0A6F5
Role: Tetradecameric ATPase cage that binds non-native clients through its apical domains and drives encapsulation by ATP binding and hydrolysis.
GroES co-chaperonin lid
Participant: Gene Product: E. coli GroES
Gene Product:
E. coli GroESUniProtKB:P0A6F9
Role: Heptameric co-chaperonin lid that caps GroEL and permits productive folding inside the GroEL cage.

Function

ATP-dependent protein folding chaperoneGO:0140662
Substrates: ATP unfolded polypeptide
Products: ADP phosphate folded polypeptide

Processes

protein foldingGO:0006457

Locations

cytosolGO:0005829

ATP-driven chaperonin chamber that encloses non-native clients and gives them a protected folding environment.

Part 2: HOCl-activated CnoX redox protection (optional)
CnoX redox quality-control pluginBiological Processcnox_redox_quality_control_plugin

Annotons

CnoX HOCl-activated chaperedoxin
cnox_holdase_chaperedoxin
Participant: Gene Product: E. coli CnoX
Gene Product:
E. coli CnoXUniProtKB:P77395

Function

holdase chaperone activity
Substrates: oxidizing non-native GroEL client protein
Products: CnoX-protected GroEL client protein

Processes

cellular response to oxidative stressGO:0034599 protein refoldingGO:0042026

Locations

cytosolGO:0005829

HOCl-activated holdase/redox-protection factor that captures oxidizing clients, protects their cysteines through reversible mixed disulfides, and can associate with GroEL outside its client-binding site.

CnoX binding to GroEL
cnox_groel_binding
Participant: Gene Product: E. coli CnoX
Gene Product:
E. coli CnoXUniProtKB:P77395

Function

protein-folding chaperone bindingGO:0051087
Substrates: GroEL apical domain

Processes

protein refoldingGO:0042026

Locations

cytosolGO:0005829

C-terminal CnoX helix binding on GroEL creates a transient redox plugin that can be released by GroES.