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dnaJ:Gene Product(s)
From EcoliWiki
| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| 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) |
|
| edit table |
Notes
Function
Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
| Qualifier | GO ID | GO term name | Reference(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0051082 |
unfolded protein binding |
GO_REF:0000002 |
IEA: Inferred from Electronic Annotation |
InterPro:IPR001305 |
F |
Seeded from EcoCyc 12.5 [5] |
complete | |
| GO:0046872 |
metal ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [6] |
complete | |||
| GO:0031072 |
heat shock protein binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc 12.5 [5] |
complete | |||
| GO:0009408 |
response to heat |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [6] |
complete | |||
| GO:0008270 |
zinc ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [6] |
complete | |||
| GO:0006950 |
response to stress |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [6] |
complete | |||
| GO:0006457 |
protein folding |
GO_REF:0000002 |
IEA: Inferred from Electronic Annotation |
InterPro:IPR001305 |
P |
Seeded from EcoCyc [6] |
complete | |
| GO:0006260 |
DNA replication |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [6] |
complete | |||
| GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc 12.5 [5] |
complete | |||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [6] |
complete | |||
| GO:0003756 |
protein disulfide isomerase activity |
IDA: Inferred from Direct Assay |
F |
Figure 4A- |
complete | |||
| GO:0005515 |
protein binding |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
| GO:0008270 |
zinc ion binding |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
| GO:0006457 |
protein folding |
IDA: Inferred from Direct Assay |
P |
complete | ||||
| GO:0042026 |
protein refolding |
IDA: Inferred from Direct Assay |
P |
complete | ||||
| GO:0051082 |
unfolded protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0042803 |
protein homodimerization activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0005624 |
membrane fraction |
IDA: Inferred from Direct Assay |
C |
complete | ||||
| GO:0005737 |
cytoplasm |
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 |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0005624 |
membrane fraction |
IDA: Inferred from Direct Assay |
C |
complete | ||||
| GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0006260 |
DNA replication |
IMP: Inferred from Mutant Phenotype |
P |
λ DNA replication affected |
complete | |||
| GO:0009408 |
response to heat |
IEP: Inferred from Expression Pattern |
P |
complete | ||||
| edit table |
Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
| Partner Type | Partner | Notes | References | Evidence |
|---|---|---|---|---|
|
Protein |
Subunits of DnaJ/DnaK/GrpE |
could be indirect | ||
|
Protein |
Experiment(s):EBI-1135319 | |||
|
Protein |
Experiment(s):EBI-1135319 | |||
|
Protein |
Experiment(s):EBI-1135319 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-881486 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-879887 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-881611, EBI-889076 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-888239, EBI-893751 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-880367 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-891381 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-890903 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-889906 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-883621, EBI-894882 | |||
|
Protein |
Experiment(s):EBI-883621 | |||
|
Protein |
Experiment(s):EBI-890903 | |||
|
Protein |
Experiment(s):EBI-890903 | |||
|
Protein |
Experiment(s):EBI-890903 | |||
|
Protein |
Experiment(s):EBI-890903 | |||
| edit table |
Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
| Compartment | Description | Evidence | Source | Notes |
|---|---|---|---|---|
| edit table |
Notes
Structure and Physical Properties
Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
| Sequence |
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) |
| edit table |
|
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures
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| Resource type | Source | Notes/Reference |
|---|---|---|
| edit table |
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
|
| ||
| edit table |
Notes
Links
| Name | URL | Comments |
|---|---|---|
| edit table |
References
See Help:References for how to manage references in EcoliWiki.
- ↑ 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)
- ↑ 2.0 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
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 5.2 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 6.0 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
- ↑ 7.0 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
- ↑ 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
- ↑ Linke K et al. (2003) The roles of the two zinc binding sites in DnaJ. J Biol Chem 278: 44457-66 PubMed EcoliWiki page
- ↑ 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
- ↑ 11.0 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
- ↑ Katayama A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem 269: 2403-13 PubMed EcoliWiki page
- ↑ 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
- ↑ 14.0 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
- ↑ Sell SM et al. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol 172: 4827-35 PubMed EcoliWiki page
- ↑ Chuang SE & Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175: 5242-52 PubMed EcoliWiki page
- ↑ 17.0 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
- ↑ 18.00 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

