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8  structures 8756  species 0  interactions 11771  sequences 58  architectures

Family: GrpE (PF01025)

Summary: GrpE

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "GrpE". More...

GrpE Edit Wikipedia article


GrpE are a family of conserved ubiquitously expressed heat shock proteins 20-30 kDa in size. Dimeric GrpE serves as the co-chaperone for Hsp70/DnaK.[1]

  1. ^ Georgopoulos, C; Welch, WJ (1993). "Role of the major heat shock proteins as molecular chaperones". Annual review of cell biology. 9: 601–34. doi:10.1146/annurev.cb.09.110193.003125. PMID 8280473.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

GrpE Provide feedback

No Pfam abstract.

Literature references

  1. Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J; , Science 1997;276:431-435.: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. PUBMED:9103205 EPMC:9103205

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000740

Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolysing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. In prokaryotes the dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold [ PUBMED:8280473 ]. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins: unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle [ PUBMED:14984054 , PUBMED:20036249 , PUBMED:22544739 , PUBMED:11580258 , PUBMED:12369934 , PUBMED:10430558 , PUBMED:22683810 , PUBMED:24269840 , PUBMED:19075746 ].

In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.

The X-ray crystal structure of GrpE in complex with the ATPase domain of DnaK revealed that GrpE is an asymmetric homodimer, bent in a manner that favours extensive contacts with only one DnaK ATPase monomer [ PUBMED:15136046 ]. GrpE does not actively compete for the atomic positions occupied by the nucleotide. GrpE and ADP mutually reduce one another's affinity for DnaK 200-fold, and ATP instantly dissociates GrpE from DnaK.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_817 (release 3.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 64
Number in full: 11771
Average length of the domain: 177.2 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 81.43 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.8 25.8
Trusted cut-off 25.8 25.8
Noise cut-off 25.6 25.7
Model length: 166
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GrpE domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044UVV1 View 3D Structure Click here
A0A077Z2A3 View 3D Structure Click here
A0A0D2GYC3 View 3D Structure Click here
A0A0H3GWG3 View 3D Structure Click here
A0A0H5S2D7 View 3D Structure Click here
A0A0K0EHN6 View 3D Structure Click here
A0A0N4UR40 View 3D Structure Click here
A0A0P0VLJ4 View 3D Structure Click here
A0A0R0J2L9 View 3D Structure Click here
A0A0R0L372 View 3D Structure Click here
A0A158Q6N1 View 3D Structure Click here
A0A175W936 View 3D Structure Click here
A0A1C1D0B6 View 3D Structure Click here
A0A1D6EAQ0 View 3D Structure Click here
A0A1D6Q4Q1 View 3D Structure Click here
A0A3P7DI12 View 3D Structure Click here
A0A3Q0KGT2 View 3D Structure Click here
A0B748 View 3D Structure Click here
A0KMI7 View 3D Structure Click here
A0LH27 View 3D Structure Click here
A1A3P4 View 3D Structure Click here
A1ANV1 View 3D Structure Click here
A1AXV2 View 3D Structure Click here
A1K4C6 View 3D Structure Click here
A1S8D5 View 3D Structure Click here
A1STE3 View 3D Structure Click here
A1TLI0 View 3D Structure Click here
A1UUC9 View 3D Structure Click here
A1VMG3 View 3D Structure Click here
A1WAR5 View 3D Structure Click here
A1WGK0 View 3D Structure Click here
A1WX32 View 3D Structure Click here
A3CQC3 View 3D Structure Click here
A3MZ85 View 3D Structure Click here
A3PA63 View 3D Structure Click here
A3QGP0 View 3D Structure Click here
A4G8D3 View 3D Structure Click here
A4I5A2 View 3D Structure Click here
A4I5A3 View 3D Structure Click here
A4SFR6 View 3D Structure Click here