GroEL

• Description: chaperonin and co-repressor for HrcA
  
  

Gene name	groEL
Synonyms
Essential	yes PubMed
Product	chaperonin, co-repressor for HrcA
Function	protein folding and re-folding
Gene expression levels in SubtiExpress: groEL
Interactions involving this protein in SubtInteract: GroEL
Metabolic function and regulation of this protein in SubtiPathways: groEL
MW, pI	57 kDa, 4.531
Gene length, protein length	1632 bp, 544 aa
Immediate neighbours	groES, ydzT/1
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

chaperones/ protein folding, heat shock proteins, essential genes, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

HrcA regulon

The gene

Basic information

• Locus tag: BSU06030

Expression

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: acts as co-repressor for HrcA

• Protein family: chaperonin (HSP60) family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-35, Arg-116, and Arg-282 PubMed
  • phosphorylated on ser/ thr/ tyr PubMed, PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions: HrcA-GroEL, GroEL-GroES

• Localization:
  • cytoplasm (according to Swiss-Prot)
  • recruited to the membrane after ethanol stress PubMed

Database entries

• Structure:

• UniProt: P28598

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: groES-groEL PubMed

• Expression browser: groEL PubMed

• Sigma factor: SigA PubMed

• Regulation: induced by heat shock (HrcA) PubMed

• Regulatory mechanism: HrcA: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:
  • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP1000 available in Jörg Stülke's lab
  • for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP1002 available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Wolfgang Schumann, Bayreuth University, Germany Homepage

References

Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

G Seydlová, P Halada, R Fišer, O Toman, A Ulrych, J Svobodová
DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress.
J Appl Microbiol: 2012, 112(4);765-74
[PubMed:22268681] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Silke Reischl, Thomas Wiegert, Wolfgang Schumann
Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE function.
J Biol Chem: 2002, 277(36);32659-67
[PubMed:12082092] [WorldCat.org] [DOI] (P p)

A Mogk, G Homuth, C Scholz, L Kim, F X Schmid, W Schumann
The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis.
EMBO J: 1997, 16(15);4579-90
[PubMed:9303302] [WorldCat.org] [DOI] (P p)

A Schulz, W Schumann
hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes.
J Bacteriol: 1996, 178(4);1088-93
[PubMed:8576042] [WorldCat.org] [DOI] (P p)

G Yuan, S L Wong
Isolation and characterization of Bacillus subtilis groE regulatory mutants: evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaK.
J Bacteriol: 1995, 177(22);6462-8
[PubMed:7592421] [WorldCat.org] [DOI] (P p)

A Schmidt, M Schiesswohl, U Völker, M Hecker, W Schumann
Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis.
J Bacteriol: 1992, 174(12);3993-9
[PubMed:1350777] [WorldCat.org] [DOI] (P p)

M Li, S L Wong
Cloning and characterization of the groESL operon from Bacillus subtilis.
J Bacteriol: 1992, 174(12);3981-92
[PubMed:1350776] [WorldCat.org] [DOI] (P p)