GroEL-GroES complex

GO:1990220 · Other · Multiprotein complex · Proposed

Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The 60kDa subunit possesses ATPase activity while the holo-enzyme is responsible for the correct folding of proteins. [GO:1990220]

Synonyms: bacterial chaperonin ATPase complex; bacterial chaperonin complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
Chaperonin Cpn60/GroEL	Protein	part of	`InterPro:IPR001844`	groEL	14 copies per asymmetric GroEL-GroES complex		ATPase chaperonin ring subunit that forms the two stacked GroEL heptameric rings. `GO:1990220` GO:1990220 defines the complex as containing a tetradecameric 60 kDa GroEL chaperonin subunit. `InterPro:IPR001844` InterPro IPR001844 is a family entry named Chaperonin Cpn60/GroEL. `PDB:1AON` RCSB maps PDB:1AON polymer entity 1 to fourteen Escherichia coli GroEL chains.
GroES chaperonin	Protein	part of	`InterPro:IPR020818`	groES	7 copies per asymmetric GroEL-GroES complex		Co-chaperonin cap subunit that forms the GroES heptamer bound to one GroEL ring. `GO:1990220` GO:1990220 defines the complex as containing a heptameric 10 kDa GroES chaperonin subunit. `InterPro:IPR020818` InterPro IPR020818 is a family entry named GroES chaperonin family. `PDB:1AON` RCSB maps PDB:1AON polymer entity 2 to seven Escherichia coli GroES chains.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

Chaperonin Cpn60/GroEL

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P0A6F5`	Chaperonin GroEL	groEL	Escherichia coli K-12 (`NCBITaxon:83333`)	REVIEWED
Role and evidence (2 references) Reviewed E. coli K-12 GroEL accession mapped by RCSB to the fourteen GroEL chains in PDB:1AON. `UniProtKB:P0A6F5` UniProtKB P0A6F5 is the reviewed Escherichia coli K-12 entry for chaperonin GroEL. `PDB:1AON` RCSB SIFTS maps PDB:1AON polymer entity 1 to UniProtKB:P0A6F5 with fourteen protein chains.

GroES chaperonin

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P0A6F9`	Co-chaperonin GroES	groES	Escherichia coli K-12 (`NCBITaxon:83333`)	REVIEWED
Role and evidence (2 references) Reviewed E. coli K-12 GroES accession mapped by RCSB to the seven GroES chains in PDB:1AON. `UniProtKB:P0A6F9` UniProtKB P0A6F9 is the reviewed Escherichia coli K-12 entry for co-chaperonin GroES. `PDB:1AON` RCSB SIFTS maps PDB:1AON polymer entity 2 to UniProtKB:P0A6F9 with seven protein chains.

Canonical examples

NCBITaxon:562 Escherichia coli — Bacterial source of the asymmetric 14-GroEL, 7-GroES GroEL-GroES/(ADP)7 crystal structure deposited as PDB:1AON. [PDB:1AON]

Functions

protein folding GO:0006457 — GroEL-GroES assists ATP-dependent folding of substrate proteins inside a transient GroEL cavity capped by GroES.
- GO:1990220 GO:1990220 defines the GroEL-GroES holoenzyme by its role in correct protein folding.
- DOI:10.1038/41944 Xu, Horwich and Sigler 1997 solved the asymmetric GroEL-GroES-(ADP)7 structure.

Physical properties

SUBUNIT_COUNT: 21 (Asymmetric Escherichia coli GroEL-GroES/(ADP)7 complex in PDB:1AON) [PDB:1AON]

Evidence

GO:1990220 Gene Ontology cellular-component term for the GroEL-GroES complex and source of its related bacterial-chaperonin synonyms.
GO:0016465 Gene Ontology cellular-component term for chaperonin ATPase complexes, the broader class that includes GroEL-GroES.
GO:0006457 Gene Ontology biological-process term for protein folding.
InterPro:IPR001844 InterPro family entry for Chaperonin Cpn60/GroEL.
InterPro:IPR020818 InterPro family entry for GroES chaperonins.
UniProtKB:P0A6F5 UniProtKB reviewed E. coli K-12 GroEL entry.
UniProtKB:P0A6F9 UniProtKB reviewed E. coli K-12 GroES entry.
DOI:10.1038/41944 Xu, Horwich and Sigler 1997, The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex, Nature.
PMID:9285585 PubMed identifier for Xu, Horwich and Sigler 1997 as reported by RCSB PDB:1AON.
PDB:1AON RCSB Protein Data Bank entry for the asymmetric Escherichia coli GroEL-GroES-(ADP)7 crystal structure from Xu, Horwich and Sigler 1997.

Curation history

2026-10-01T17:00:42Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-10-01T17:03:20Z codex · EXPANDED_RECORD — Added GO synonymy and chaperonin-ATPase parentage, GroEL and GroES components grounded to exact InterPro families with E. coli UniProt examples, an E. coli PDB:1AON canonical example, protein-folding function evidence, PDB-backed stoichiometry, and DOI/PMID/PDB evidence.

Source: data/structures/other/groel_groes_complex.yaml