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dnaJ: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

DnaJ

Synonyms

chaperone Hsp40, co-chaperone with DnaK[1], B0015[2][1], GrpC[2][1], GroP[2][1], DnaJ[2][1]

Product description

chaperone with DnaK; heat shock protein[2][3];

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

DnaK co-chaperone; stress-related DNA biosynthesis, responsive to heat shock; binds Zn(II)[4]

EC number (for enzymes)


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

IEA: Inferred from Electronic Annotation

InterPro:IPR001305
InterPro:IPR002939
InterPro:IPR003095
InterPro:IPR008971
InterPro:IPR012724
HAMAP:MF_01152

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [6]

complete

GO:0031072

heat shock protein binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001305
InterPro:IPR001623
InterPro:IPR003095

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0009408

response to heat

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012724

P

Seeded from EcoCyc [6]

complete

GO:0008270

zinc ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0862

F

Seeded from EcoCyc [6]

complete

GO:0006950

response to stress

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0346

P

Seeded from EcoCyc [6]

complete

GO:0006457

protein folding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001305
InterPro:IPR002939
InterPro:IPR003095
InterPro:IPR008971
InterPro:IPR012724

P

Seeded from EcoCyc [6]

complete

GO:0006260

DNA replication

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0235

P

Seeded from EcoCyc [6]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [5]

complete

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012724

F

Seeded from EcoCyc [6]

complete

GO:0003756

protein disulfide isomerase activity

PMID:7559385[7]

IDA: Inferred from Direct Assay

F

Figure 4A-

complete

GO:0005515

protein binding

PMID:9860950[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0008270

zinc ion binding

PMID:12941935[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0006457

protein folding

PMID:7559385[7]

IDA: Inferred from Direct Assay

P

complete

GO:0042026

protein refolding

PMID:7559385[7]

IDA: Inferred from Direct Assay

P

complete

GO:0051082

unfolded protein binding

PMID:7559385[7]

IDA: Inferred from Direct Assay

F

complete

GO:0042803

protein homodimerization activity

PMID:15849180[10]

IDA: Inferred from Direct Assay

F

complete

GO:0005624

membrane fraction

PMID:6220698[11]

IDA: Inferred from Direct Assay

C

complete

GO:0005737

cytoplasm

PMID:6220698[11]

IDA: Inferred from Direct Assay

C

DnaJ can be detected in the soluble fraction as well as being loosely membrane-associated.

complete

GO:0008270

zinc ion binding

PMID:11985624[12]

IDA: Inferred from Direct Assay

F

complete

GO:0005624

membrane fraction

PMID:3889001[13]

IDA: Inferred from Direct Assay

C

complete

GO:0008270

zinc ion binding

PMID:8662861[14]

IDA: Inferred from Direct Assay

F

complete

GO:0006260

DNA replication

PMID:2144273[15]

IMP: Inferred from Mutant Phenotype

P

λ DNA replication affected

complete

GO:0009408

response to heat

PMID:8349564[16]

IEP: Inferred from Expression Pattern

P

complete

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

mnmG

PMID:16606699[17]

Experiment(s):EBI-1135319

Protein

sucB

PMID:16606699[17]

Experiment(s):EBI-1135319

Protein

pdxB

PMID:16606699[17]

Experiment(s):EBI-1135319

Protein

aceE

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

add

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

atpD

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

clpA

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

deaD

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-881486

Protein

dnaK

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

gatY

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

imp

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

infB

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

malT

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-879887

Protein

metK

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-881611, EBI-889076

Protein

mreB

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-888239, EBI-893751

Protein

mukB

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

narG

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-880367

Protein

pstB

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-891381

Protein

recA

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

relE

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rho

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rplA

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rplJ

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rplS

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rplV

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rpoC

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rpsB

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rpsE

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rpsJ

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-890903

Protein

rpsM

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

srmB

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-889906

Protein

trxC

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

tufA

PMID:15690043[18]

Experiment(s):EBI-883621, EBI-894882

Protein

yjbJ

PMID:15690043[18]

Experiment(s):EBI-883621

Protein

rplX

PMID:15690043[18]

Experiment(s):EBI-890903

Protein

rpsF

PMID:15690043[18]

Experiment(s):EBI-890903

Protein

rpsN

PMID:15690043[18]

Experiment(s):EBI-890903

Protein

rplW

PMID:15690043[18]

Experiment(s):EBI-890903

Notes

Localization

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

CompartmentDescriptionEvidenceSourceNotes

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

MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS
QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN
MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ
QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP
AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG
KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRS
KSFFDGVKKF FDDLTR
Length

376

Mol. Wt

41.099 kDa

pI

8.0 (calculated)

Extinction coefficient

14,900 - 16,150 (calc based on 10 Y, W, and 10 C residues)


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:P08622

Motif

zinc finger

PMID:8662861[14]



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

Structures
Models

View models at:

Structure figures

Notes

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

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:EG10240-MONOMER

UniProt (EcoliWiki Page)

UniProt:P08622

PFAM (EcoliWiki Page)

PFAM:PF00226

RefSeq (EcoliWiki Page)

RefSeq:NP_414556


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 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 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 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 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  6. 6.0 6.1 6.2 6.3 6.4 6.5 6.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  7. 7.0 7.1 7.2 7.3 de Crouy-Chanel A et al. (1995) A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. J Biol Chem 270: 22669-72 PubMed EcoliWiki page
  8. Suh WC et al. (1998) Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc Natl Acad Sci U S A 95: 15223-8 PubMed EcoliWiki page
  9. Linke K et al. (2003) The roles of the two zinc binding sites in DnaJ. J Biol Chem 278: 44457-66 PubMed EcoliWiki page
  10. Shi YY et al. (2005) The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity: a small angle X-ray scattering study in solution. J Biol Chem 280: 22761-8 PubMed EcoliWiki page
  11. 11.0 11.1 Zylicz M et al. (1983) Escherichia coli dnaJ- and dnaK-gene products: synthesis in minicells and membrane-affinity. Biochem Biophys Res Commun 110: 176-80 PubMed EcoliWiki page
  12. Katayama A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem 269: 2403-13 PubMed EcoliWiki page
  13. Zylicz M et al. (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J Biol Chem 260: 7591-8 PubMed EcoliWiki page
  14. 14.0 14.1 Banecki B et al. (1996) Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone. J Biol Chem 271: 14840-8 PubMed EcoliWiki page
  15. Sell SM et al. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol 172: 4827-35 PubMed EcoliWiki page
  16. Chuang SE & Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175: 5242-52 PubMed EcoliWiki page
  17. 17.0 17.1 17.2 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
  18. 18.00 18.01 18.02 18.03 18.04 18.05 18.06 18.07 18.08 18.09 18.10 18.11 18.12 18.13 18.14 18.15 18.16 18.17 18.18 18.19 18.20 18.21 18.22 18.23 18.24 18.25 18.26 18.27 18.28 18.29 18.30 18.31 18.32 18.33 18.34 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page

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