groL chaperonin GroEL [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Go to the top of the page Help

Official Symbol: groL
Official Full Name: chaperonin GroEL
Primary source: ECOCYC:EG10599
Locus tag: b4143
See related: ASAP:ABE-0013568
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK4137; groEL; mopA
Summary: groL is an essential gene. [More information is available at EcoGene: EG10599]. The Escherichia coli chaperone protein GroEL (Hsp60) and its regulator GroES are necessary for the proper folding of certain proteins , . [More information is available at EcoCyc: EG10599].
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Sequence:: NC_000913.3 (4371025..4372671)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Human embryo models are getting more realistic - raising ethical questions.
Title: Human embryo models are getting more realistic - raising ethical questions.
In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
Title: In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues.
Title: The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues.
While GroEL and GroES increases the folding rate of PepQ by over 15-fold, the slow spontaneous folding of PepQ is not caused by aggregation.
Title: GroEL actively stimulates folding of the endogenous substrate protein PepQ.
study confirmed the altered GroEL dependence of green fluorescent protein variants with in vitro folding assays; mutations at positions predicted to be highly frustrated were found to correlate with decreased GroEL dependence; conversely, mutations at positions with low frustration were found to correlate with increased GroEL dependence
Title: Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
Data suggest that neither DnaK nor GroEL singly can modulate sigma32 stability in vivo; there is ordered network between them, where GroEL acts upstream of DnaK.
Title: GroEL to DnaK chaperone network behind the stability modulation of σ(32) at physiological temperature in Escherichia coli.
In the case of GroEL, individualisation of monomers thus leads to individualisation of homomultimeric protein complexes, effectively providing the prerequisites for evolving an orthogonal intracellular GroEL folding machine.
Title: Towards functional orthogonalisation of protein complexes: individualisation of GroEL monomers leads to distinct quasihomogeneous single rings.
Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature-dependent proteolysis of the latter.
Title: Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC).
Investigated the role of the surface-associated GroEL in the binding of E. coli to macrophages. Results showed that GroEL on E. coli was recognized by LOX-1 on macrophages, leading to the phagocytosis of pathogen by macrophages.
Title: Surface-associated GroEL facilitates the adhesion of Escherichia coli to macrophages through lectin-like oxidized low-density lipoprotein receptor-1.
Nuclear magnetic resonance (NMR) observation of the uniformly (2) H,(15) N-labeled stringent 33-kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1.
Title: Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.

Submit: New GeneRIF Correction See all GeneRIFs (38)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

General protein information

Go to the top of the page Help

Preferred Names: chaperonin GroEL

NP_418567.1

EC 5.6.1.7

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

4371025..4372671

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_418567.1 chaperonin GroEL [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_418567.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A376ZKM4

Conserved Domains (1) summary

PRK00013
Location:2 → 530

groEL; chaperonin GroEL; Reviewed