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ECOLI:DNAK

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) dnaK (synonyms: groP, grpF, seg)
Protein Name(s) Chaperone protein DnaK

HSP70 Heat shock 70 kDa protein Heat shock protein 70

External Links
UniProt P0A6Y8
EMBL K01298
U00096
AP009048
D10765
M12565
PIR A03311
RefSeq NP_414555.1
YP_488320.1
PDB 1BPR
1DG4
1DKG
1DKX
1DKY
1DKZ
1Q5L
2BPR
2KHO
3DPO
3DPP
3DPQ
3QNJ
4B9Q
4E81
4EZN
4EZO
4EZP
4EZQ
4EZR
4EZS
4EZT
4EZU
4EZV
4EZW
4EZX
4EZY
4EZZ
4F00
4F01
4HY9
4HYB
4JN4
4JNE
4JNF
4JWC
4JWD
4JWE
4JWI
4R5G
4R5I
4R5J
4R5K
4R5L
PDBsum 1BPR
1DG4
1DKG
1DKX
1DKY
1DKZ
1Q5L
2BPR
2KHO
3DPO
3DPP
3DPQ
3QNJ
4B9Q
4E81
4EZN
4EZO
4EZP
4EZQ
4EZR
4EZS
4EZT
4EZU
4EZV
4EZW
4EZX
4EZY
4EZZ
4F00
4F01
4HY9
4HYB
4JN4
4JNE
4JNF
4JWC
4JWD
4JWE
4JWI
4R5G
4R5I
4R5J
4R5K
4R5L
ProteinModelPortal P0A6Y8
SMR P0A6Y8
BioGrid 849153
DIP DIP-35751N
IntAct P0A6Y8
MINT MINT-7259066
STRING 511145.b0014
TCDB 1.A.33.1.2
PhosSite P010484
SWISS-2DPAGE P0A6Y8
PaxDb P0A6Y8
PRIDE P0A6Y8
EnsemblBacteria AAC73125
BAB96589
GeneID 12930526
944750
KEGG ecj:Y75_p0014
eco:b0014
PATRIC 32115121
EchoBASE EB0237
EcoGene EG10241
eggNOG COG0443
HOGENOM HOG000228136
InParanoid P0A6Y8
KO K04043
OMA FFGKDPH
OrthoDB EOG6JMMSV
PhylomeDB P0A6Y8
BioCyc EcoCyc:EG10241-MONOMER
ECOL316407:JW0013-MONOMER
EvolutionaryTrace P0A6Y8
PRO PR:P0A6Y8
Proteomes UP000000318
UP000000625
Genevestigator P0A6Y8
GO GO:0005737
GO:0016020
GO:0005886
GO:0043531
GO:0005524
GO:0044183
GO:0051082
GO:0008270
GO:0034620
GO:0070389
GO:0051085
GO:0006260
GO:0006461
GO:0043241
GO:0043335
GO:0009408
Gene3D 1.20.1270.10
2.60.34.10
HAMAP MF_00332
InterPro IPR012725
IPR018181
IPR029048
IPR029047
IPR013126
Pfam PF00012
PRINTS PR00301
SUPFAM SSF100920
SSF100934
TIGRFAMs TIGR02350
PROSITE PS00297
PS00329
PS01036

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0065003

protein-containing complex assembly

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051087

chaperone binding

PMID:9103205[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P08622

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:9103205[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051787

misfolded protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:95835
PANTHER:PTN002321897
RGD:2843
UniProtKB:P11021

F

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000000905
SGD:S000001106
SGD:S000001556
SGD:S000002388
SGD:S000003571
SGD:S000003947
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8
UniProtKB:P0DMV9

F

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:105384
PANTHER:PTN002321897
RGD:621725
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

F

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
SGD:S000000004
SGD:S000000756
SGD:S000003806
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

P

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000184706
PANTHER:PTN002321897
RGD:621725
SGD:S000000905
UniProtKB:A5I640
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

P

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1311806
UniProtKB:K7NTP5
UniProtKB:O73885
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:Q8IB24

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
EcoGene:EG13653
PANTHER:PTN002321897
PomBase:SPAC664.11
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000002388
SGD:S000003571
SGD:S000003806
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11021
UniProtKB:P11142
WB:WBGene00002005

F

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1593284
RGD:2840
SGD:S000001556
SGD:S000003571
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
PANTHER:PTN000453405

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
FB:FBgn0266599
MGI:MGI:105384
MGI:MGI:96244
PANTHER:PTN002321897
PomBase:SPCC1739.13
RGD:1311806
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000905
SGD:S000001106
SGD:S000002388
SGD:S000003947
UniProtKB:O73885
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066
UniProtKB:P22953
UniProtKB:Q27975
UniProtKB:Q8IB24
WB:WBGene00002005

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
PANTHER:PTN002321897
RGD:621725
SGD:S000001556
SGD:S000003947
TAIR:locus:2101222
TAIR:locus:2121022
TAIR:locus:2135897
TAIR:locus:2144801
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:Q7SX63

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:8349564[4]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:11985624[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0065003

protein-containing complex assembly

PMID:2525130[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0065003

protein-containing complex assembly

PMID:2525129[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:10458167[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:7900997[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:2203539[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9145101[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:10380927[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043531

ADP binding

PMID:7776367[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043531

ADP binding

PMID:19439666[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:7900997[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:2203539[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032984

protein-containing complex disassembly

PMID:2543679[15]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032984

protein-containing complex disassembly

PMID:2525130[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016989

sigma factor antagonist activity

PMID:8599944[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:7900997[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:7023474[17]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[18]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:7776367[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1903507

negative regulation of nucleic acid-templated transcription

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0016989

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012725

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012725

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012725

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000084064

F

Seeded From UniProt

complete

GO:0016234

cytoplasm

PMID:15866952[21]

ECO:0000314

C

Figure 1. Shows strong Dnak chaperone system localization to the inclusion body surfaces of fusion protein VP1LAC while low levels were detected in the cytoplasm.

complete
CACAO 11033

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

GO:0005524

ATP binding

PMID:10521435[22]

ECO:0000021

F

DnaK and DnaJ bind under certain circumstances- the abstract mentions that they have been shown to be co-chaperones. Figure 1, graph 1 demonstrates binding assays using immobilized DnaK on a sensor chip. The binding of DnaK to DnaJ occurs only in the presence of ATP, and not any other form of nucleotide. While this is not a direct analysis of the ATP-binding domain, from the graph it is possible to infer that DnaK requires the presence of ATP to bind DnaJ, and that the ATP is binding to DnaK (since it was only present in solution during the process of immobilizing DnaK, not when the DnaJ was added).

Missing: with/from
CACAO 4658

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0235

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Harrison, CJ et al. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 431-5 PubMed GONUTS page
  2. ↑ 2.0 2.1 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 GONUTS page
  3. ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
  5. ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page
  6. ↑ 6.0 6.1 Dodson, M et al. (1989) Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda. Protein association and disassociation reactions responsible for localized initiation of replication. J. Biol. Chem. 264 10719-25 PubMed GONUTS page
  7. ↑ Alfano, C & McMacken, R (1989) Ordered assembly of nucleoprotein structures at the bacteriophage lambda replication origin during the initiation of DNA replication. J. Biol. Chem. 264 10699-708 PubMed GONUTS page
  8. ↑ Deuerling, E et al. (1999) Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400 693-6 PubMed GONUTS page
  9. ↑ 9.0 9.1 9.2 Schröder, H et al. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12 4137-44 PubMed GONUTS page
  10. ↑ 10.0 10.1 Skowyra, D et al. (1990) The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62 939-44 PubMed GONUTS page
  11. ↑ Rüdiger, S et al. (1997) Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4 342-9 PubMed GONUTS page
  12. ↑ Teter, SA et al. (1999) Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97 755-65 PubMed GONUTS page
  13. ↑ 13.0 13.1 McCarty, JS et al. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249 126-37 PubMed GONUTS page
  14. ↑ Bertelsen, EB et al. (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl. Acad. Sci. U.S.A. 106 8471-6 PubMed GONUTS page
  15. ↑ Alfano, C & McMacken, R (1989) Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication. J. Biol. Chem. 264 10709-18 PubMed GONUTS page
  16. ↑ Gamer, J et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15 607-17 PubMed GONUTS page
  17. ↑ Neidhardt, FC & VanBogelen, RA (1981) Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem. Biophys. Res. Commun. 100 894-900 PubMed GONUTS page
  18. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  19. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  20. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  21. ↑ Carrió, MM & Villaverde, A (2005) Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187 3599-601 PubMed GONUTS page
  22. ↑ Suh, WC et al. (1999) Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274 30534-9 PubMed GONUTS page
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