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dnaK:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

DnaK

Synonyms

chaperone Hsp70, co-chaperone with DnaJ[1], B0014[2][1], GrpC[2][1], GrpF[2][1], Seg[2][1], GroP[2][1], DnaL[2][1], DnaK[2][1]

Product description

chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins[2][3];

Component of DnaJ/DnaK/GrpE[2][3]

Hsp70 molecular chaperone, heat-inducible[4]

EC number (for enzymes)


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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0051082

unfolded protein binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012725

F

Seeded from EcoCyc [5]

complete

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc [5]

complete

GO:0006950

response to stress

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0346

P

Seeded from EcoCyc [5]

complete

GO:0006457

protein folding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012725

P

Seeded from EcoCyc [5]

complete

GO:0006260

DNA replication

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0235

P

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001023
InterPro:IPR012725
SP_KW:KW-0067
HAMAP:MF_00332

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [5]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0A853

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0AAI5

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0AB71

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0AC38

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0AC81

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0ACX3

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0ADX9

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P12282

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P23721

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P28304

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P37342

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P45578

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P69924

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16139413[8]

IPI: Inferred from Physical Interaction

UniProtKB:P21513

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P00634

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P00811

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6Z3

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0A9Q9

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0AG80

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0C0V0

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P10346

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P16700

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P17117

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P28635

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P30011

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P36677

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P37024

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P37685

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P46853

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P62623

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P68919

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P69822

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:P76002

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:Q46796

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:16606699[9]

IPI: Inferred from Physical Interaction

UniProtKB:Q46906

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005737

cytoplasm

PMID:16858726[10]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0005886

plasma membrane

GO_REF:0000004
GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997
SP_KW:KW-1003
SP_SL:SL-0037

C

Seeded from EcoCyc [5]

complete

GO:0006970

response to osmotic stress

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0000910

cytokinesis

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0008270

zinc ion binding

PMID:11985624[11]

IDA: Inferred from Direct Assay

F

complete

GO:0009408

response to heat

PMID:8349564[12]

IEP: Inferred from Expression Pattern

P

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner TypePartnerNotesReferencesEvidence

Protein

Subunits of DnaJ/DnaK/GrpE

could be indirect

Protein

htpG

PMID:16606699[9]

Experiment(s):EBI-1135316

Protein

aphA

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

gadA

PMID:15690043[7]

Experiment(s):EBI-883577, EBI-888455, EBI-893820

Protein

grpE

PMID:15690043[7]

Experiment(s):EBI-883577, EBI-881166, EBI-888219, EBI-890853

Protein

lon

PMID:15690043[7]

Experiment(s):EBI-883577

Protein

rplF

PMID:15690043[7]

Experiment(s):EBI-883577

Protein

rplJ

PMID:15690043[7]

Experiment(s):EBI-883577

Protein

rpsB

PMID:15690043[7]

Experiment(s):EBI-883577, EBI-890853

Protein

tufA

PMID:15690043[7]

Experiment(s):EBI-883577, EBI-894882, EBI-890853

Protein

yibA

PMID:15690043[7]

Experiment(s):EBI-883577

Protein

ydcR

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

ydfJ

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

entB

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

fabB

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

hisC

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

hscA

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

narQ

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

pepB

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

proS

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

rplI

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

rplS

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

rpmG

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

sapA

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

tdcG

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

dcuD

PMID:15690043[7]

Experiment(s):EBI-890853

Protein

yihM

PMID:15690043[7]

Experiment(s):EBI-890853

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Cytoplasm

PMID:9298646[13], PMID:1396676[14], PMID:7783627[15]

EchoLocation:dnaK


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Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD
HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
Length

638

Mol. Wt

69.115 kDa

pI

4.7 (calculated)

Extinction coefficient

15,930 - 16,055 (calc based on 7 Y, 1 W, and 1 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

TypeResiduesDescriptionNotesReferences

Initiator Methionine

1

Removed

UniProt:P0A6Y8

Modification Site

453

phosphorylation site at S453

probability greater than 75%

PMID:17938405[16]

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rectanglerectanglerectanglerectanglerectanglerectanglemotifs

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures
  • Representative Escherichia coli K-12 structure:
    2KHO|A
    1-605 of 638 residues (E-value: 4e-316) (Percent Identity: 99.83)
  • Representative homolog:
    1DKX|A ()
    1-219 of 638 residues (E-value: 3e-110) (Percent Identity: 99.54)
  • View the PDB Table for dnaK
Models

View models at:

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Structure figures

Notes

Like other Hsp70 chaperones, dnaK consists of two domains: and N-terminal ATPase domain, a substrate binding domain, and a short DnaJ binding domain[17]. Structures

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:EG10241-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P0A6Y8

UniProt (EcoliWiki Page)

UniProt:P0A6Y8

PFAM (EcoliWiki Page)

PFAM:PF00012

RefSeq (EcoliWiki Page)

RefSeq:NP_414555


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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 7.11 7.12 7.13 7.14 7.15 7.16 7.17 7.18 7.19 7.20 7.21 7.22 7.23 7.24 7.25 7.26 7.27 7.28 7.29 7.30 7.31 7.32 7.33 7.34 7.35 7.36 7.37 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
  8. ↑ Regonesi ME et al. (2006) Analysis of the Escherichia coli RNA degradosome composition by a proteomic approach. Biochimie 88: 151-61 PubMed EcoliWiki page
  9. ↑ 9.00 9.01 9.02 9.03 9.04 9.05 9.06 9.07 9.08 9.09 9.10 9.11 9.12 9.13 9.14 9.15 9.16 9.17 9.18 9.19 9.20 9.21 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  10. ↑ Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed EcoliWiki page
  11. ↑ Katayama A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem 269: 2403-13 PubMed EcoliWiki page
  12. ↑ Chuang SE & Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175: 5242-52 PubMed EcoliWiki page
  13. ↑ Link AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18: 1259-313 PubMed EcoliWiki page
  14. ↑ Schmid D et al. (1992) Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK. Eur J Biochem 208: 699-704 PubMed EcoliWiki page
  15. ↑ Freestone P et al. (1995) Identification of phosphoproteins in Escherichia coli. Mol Microbiol 15: 573-80 PubMed EcoliWiki page
  16. ↑ Macek B et al. (2007) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics PubMed EcoliWiki page
  17. ↑ Genevaux P et al. (2007) The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol Microbiol 66: 840-57 PubMed EcoliWiki page

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