groEL

Gene Description

GroEL (Cpn60/Hsp60; locus PP_1361) is the Group I bacterial chaperonin of Pseudomonas putida KT2440. It is an ~800 kDa cytoplasmic complex assembled from two stacked heptameric rings (a tetradecamer) that, together with its co-chaperonin GroES (PP_1360, a heptameric lid), forms the GroEL-GroES folding machine. GroEL binds non-native polypeptides via hydrophobic surfaces in its apical domains and hydrolyzes ATP at its equatorial domains; ATP and GroES binding enclose the substrate in a hydrophilic nano-cage that promotes productive folding, after which the folded product is released through an ATP-driven allosteric cycle. It assists the folding and refolding of newly synthesized and stress-denatured cytosolic proteins, preventing aggregation and supporting recovery from proteotoxic stress. In P. putida the groESL operon is part of the RpoH (sigma-32) heat-shock regulon and is induced by heat, solvent/aromatic exposure, and elevated pressure/oxygen, reflecting its central role in maintaining proteostasis. EC 5.6.1.7.

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: GroEL binds and hydrolyzes ATP at its equatorial domains to drive the folding cycle; the UniProt record annotates multiple ATP-binding residues. Reason: ATP binding is a well-established, conserved molecular function of GroEL and is directly supported by structural and biochemical evidence across the chaperonin family.
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: GroEL is a soluble cytoplasmic chaperonin; in situ cryo-electron tomography has directly visualized GroEL-GroES complexes inside bacterial cells. Reason: Cytoplasmic localization is correct and well supported for bacterial GroEL.
GO:0006457 protein folding	IEA GO_REF:0000002	ACCEPT	Summary: Assisting protein folding is the core biological process of GroEL, which encapsulates non-native substrates and provides an environment optimized to promote folding. Reason: Directly captures the central biological role of the chaperonin and is consistent with the UniProt FUNCTION annotation and extensive literature.
GO:0042026 protein refolding	IEA GO_REF:0000120	ACCEPT	Summary: GroEL refolds stress-denatured proteins; in P. putida it is induced under heat, solvent, and pressure stress as part of the RpoH regulon to restore proteostasis. Reason: Protein refolding is an accurate and more specific aspect of GroEL function, complementing the broader protein folding term.
GO:0140662 ATP-dependent protein folding chaperone	IEA GO_REF:0000002	ACCEPT	Summary: GroEL is the prototypical ATP-dependent (chaperonin) folding machine, coupling ATP binding/hydrolysis to substrate encapsulation and folding with its co-chaperonin GroES. Reason: This is the most precise molecular function term for GroEL and is strongly supported; it represents a core function of the gene.

Core Functions

ATP-dependent chaperonin that mediates the folding and refolding of non-native cytosolic polypeptides, preventing aggregation, by encapsulating substrates in the GroEL-GroES nano-cage and coupling folding to an ATP-driven allosteric cycle.

Molecular Function:

ATP-dependent protein folding chaperone

Directly Involved In:

protein folding

Supporting Evidence:

GO_REF:0000002
GroEL annotated as ATP-dependent protein folding chaperone and involved in protein folding via InterPro Cpn60/GroEL records.
PMID:39169181
GroEL forms a double-ring tetradecamer; apical domains bind non-native substrates and equatorial domains bind/hydrolyze ATP, with GroES capping to form a protected folding chamber in the cytosol.

Gene Description

Existing Annotations Review

Core Functions

ATP-dependent chaperonin that mediates the folding and refolding of non-native cytosolic polypeptides, preventing aggregation, by encapsulating substrates in the GroEL-GroES nano-cage and coupling folding to an ATP-driven allosteric cycle.

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