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Escherichia coli K-12 substr. MG1655 Polypeptide: nucleotide exchange factor GrpE



Gene: grpE Accession Numbers: EG10416 (EcoCyc), b2614, ECK2610

Synonyms: heat shock protein GrpE

Regulation Summary Diagram: ?

Component of: DnaK-DnaJ-GrpE chaperone system (summary available)

Summary:
GrpE has been shown to be essential for regulation of release of ADP and Pi from DnaK, providing further stimulation for the turnover of ATP [Liberek91]. It has also been shown that GrpE acts as a thermosensor in that at high temperatures there is a decreased efficacy of GrpE in catalyzing ATP/ADP turnover [Grimshaw03].

Review: [Harrison03]

Gene Citations: [Lipinska88]

Locations: cytosol

Map Position: [2,748,137 <- 2,748,730] (59.23 centisomes)
Length: 594 bp / 197 aa

Molecular Weight of Polypeptide: 21.798 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008598 , CGSC:660 , DIP:DIP-6141N , DisProt:DP00103 , EchoBASE:EB0411 , EcoGene:EG10416 , EcoliWiki:b2614 , Mint:MINT-1225400 , ModBase:P09372 , OU-Microarray:b2614 , PortEco:grpE , PR:PRO_000022840 , Pride:P09372 , Protein Model Portal:P09372 , RefSeq:NP_417104 , RegulonDB:EG10416 , SMR:P09372 , String:511145.b2614 , UniProt:P09372

Relationship Links: InterPro:IN-FAMILY:IPR000740 , InterPro:IN-FAMILY:IPR009012 , InterPro:IN-FAMILY:IPR013805 , Panther:IN-FAMILY:PTHR21237 , PDB:Structure:1DKG , Pfam:IN-FAMILY:PF01025 , Prints:IN-FAMILY:PR00773 , Prosite:IN-FAMILY:PS01071

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Chuang93]
GO:0043335 - protein unfolding Inferred from experiment [Sharma10a]
GO:0006457 - protein folding Inferred by computational analysis [GOA01]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
GO:0050790 - regulation of catalytic activity Inferred by computational analysis [GOA01]
Molecular Function: GO:0000774 - adenyl-nucleotide exchange factor activity Inferred by computational analysis [GOA01]
GO:0042803 - protein homodimerization activity Inferred by computational analysis [GOA01]
GO:0051087 - chaperone binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, Lasserre06]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

MultiFun Terms: cell processes cell division
extrachromosomal prophage genes and phage related functions
information transfer protein related chaperoning, repair (refolding)

Essentiality data for grpE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of: DnaK-DnaJ-GrpE chaperone system

Synonyms: Hsp70 chaperone system

Subunit composition of DnaK-DnaJ-GrpE chaperone system = [DnaJ][DnaK][GrpE]
         chaperone protein DnaJ = DnaJ (summary available)
         chaperone protein DnaK = DnaK (extended summary available)
         nucleotide exchange factor GrpE = GrpE (summary available)

Summary:
The DnaK system of E. coli (DnaK-DnaJ-GrpE) is a homolog of the eukaryotic Hsp70 chaperone system. Hsp70 chaperones assist in protein folding processes within the cell including folding and assembly of newly synthesized proteins, refolding of misfolded and aggregated proteins and translocation of secretory proteins. Hsp70 proteins (DnaK in E. coli K-12) act in conjunction with co-chaperones of the J-domain family (DnaJ in E. coli K-12) and nucleotide exchange factors (GrpE in E. coli K-12) (reviewed by [Mayer05]).


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 73
[Gelinas04, UniProt11a]
Alternate sequence: R → A; UniProt: Great decrease in ability to interact with dnaK.
Mutagenesis-Variant 74
[Gelinas04, UniProt11a]
Alternate sequence: R → A; UniProt: Great decrease in ability to interact with dnaK.
Mutagenesis-Variant 82
[Gelinas04, UniProt11a]
Alternate sequence: K → A; UniProt: Great decrease in ability to interact with dnaK.
Mutagenesis-Variant 86
[Gelinas03, UniProt11a]
Alternate sequence: F → A; UniProt: No effect in ability to interact with dnaK.
Acetylation-Modification 90
[Yu08a]
 
Mutagenesis-Variant 104
[Gelinas04, UniProt11a]
Alternate sequence: R → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 107
[Gelinas04, UniProt11a]
Alternate sequence: E → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 108
[Gelinas04, UniProt11a]
Alternate sequence: V → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 122
[Harrison97, UniProt11a]
Alternate sequence: G → D; UniProt: Temperature-sensitive phenotype.
Mutagenesis-Variant 149
[Gelinas04, UniProt11a]
Alternate sequence: L → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 151
[Gelinas04, UniProt11a]
Alternate sequence: P → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 155
[Gelinas04, UniProt11a]
Alternate sequence: Q → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 157
[Gelinas04, UniProt11a]
Alternate sequence: I → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 159
[Gelinas04, UniProt11a]
Alternate sequence: M → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 174
[Gelinas04, UniProt11a]
Alternate sequence: M → A; UniProt: No effect in ability to interact with dnaK.
Mutagenesis-Variant 183
[Gelinas04, Gelinas03, UniProt11a]
Alternate sequence: R → A; UniProt: Loss of ability to interact with dnaK.
Amino-Acid-Site 183
[UniProt10]
UniProt: Interaction with dnaK; Sequence Annotation Type: site;
Mutagenesis-Variant 186
[UniProt10]
Alternate sequence: R → A; UniProt: No effect in ability to interact with dnaK;
Mutagenesis-Variant 189
[UniProt10]
Alternate sequence: M → A; UniProt: No effect in ability to interact with dnaK;
Mutagenesis-Variant 192
[Gelinas04, Gelinas03, UniProt11a]
Alternate sequence: V → A; UniProt: Loss of ability to interact with dnaK.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2614 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10416; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Chuang93: Chuang SE, Blattner FR (1993). "Characterization of twenty-six new heat shock genes of Escherichia coli." J Bacteriol 175(16);5242-52. PMID: 8349564

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gelinas03: Gelinas AD, Toth J, Bethoney KA, Langsetmo K, Stafford WF, Harrison CJ (2003). "Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular thermosensor." Biochemistry 42(30);9050-9. PMID: 12885238

Gelinas04: Gelinas AD, Toth J, Bethoney KA, Stafford WF, Harrison CJ (2004). "Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation." J Mol Biol 339(2);447-58. PMID: 15136046

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Grimshaw03: Grimshaw JP, Jelesarov I, Siegenthaler RK, Christen P (2003). "Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures." J Biol Chem 278(21);19048-53. PMID: 12639955

Harrison03: Harrison C (2003). "GrpE, a nucleotide exchange factor for DnaK." Cell Stress Chaperones 8(3);218-24. PMID: 14984054

Harrison97: Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J (1997). "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK." Science 276(5311);431-5. PMID: 9103205

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Liberek91: Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M (1991). "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK." Proc Natl Acad Sci U S A 88(7);2874-8. PMID: 1826368

Lipinska88: Lipinska B, King J, Ang D, Georgopoulos C (1988). "Sequence analysis and transcriptional regulation of the Escherichia coli grpE gene, encoding a heat shock protein." Nucleic Acids Res 1988;16(15);7545-62. PMID: 3045760

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Mayer05: Mayer MP, Bukau B (2005). "Hsp70 chaperones: cellular functions and molecular mechanism." Cell Mol Life Sci 62(6);670-84. PMID: 15770419

Sharma10a: Sharma SK, De los Rios P, Christen P, Lustig A, Goloubinoff P (2010). "The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase." Nat Chem Biol 6(12);914-20. PMID: 20953191

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Yu08a: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Other References Related to Gene Regulation

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Wade06: Wade JT, Roa DC, Grainger DC, Hurd D, Busby SJ, Struhl K, Nudler E (2006). "Extensive functional overlap between sigma factors in Escherichia coli." Nat Struct Mol Biol 13(9);806-14. PMID: 16892065

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC13A.