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P0A6Y8 (DNAK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein DnaK
Alternative name(s):
HSP70
Heat shock 70 kDa protein
Heat shock protein 70
Gene names
Name:dnaK
Synonyms:groP, grpF, seg
Ordered Locus Names:b0014, JW0013
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock. HAMAP-Rule MF_00332

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein Ref.16.

Post-translational modification

Autophosphorylated; GrpE inhibits the autophosphorylation. Ref.11 Ref.12 Ref.13

Disruption phenotype

Non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at all at 43 degrees) and strain background. Ref.15

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processDNA replication
Stress response
   Cellular componentCell inner membrane
Cell membrane
Cytoplasm
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to unfolded protein

Inferred from direct assay PubMed 2203539PubMed 7900997. Source: EcoCyc

chaperone cofactor-dependent protein refolding

Inferred from direct assay PubMed 2203539PubMed 7900997. Source: EcoCyc

chaperone mediated protein folding requiring cofactor

Inferred from mutant phenotype PubMed 10458167. Source: EcoCyc

protein complex assembly

Inferred from direct assay PubMed 2525129PubMed 2525130. Source: EcoCyc

protein complex disassembly

Inferred from direct assay PubMed 2525130PubMed 2543679. Source: EcoCyc

protein unfolding

Inferred from direct assay PubMed 20953191. Source: EcoCyc

response to heat

Inferred from direct assay PubMed 7023474PubMed 7900997. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16858726. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16858726. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionADP binding

Inferred from direct assay PubMed 19439666PubMed 7776367. Source: EcoCyc

ATP binding

Inferred from direct assay PubMed 7776367. Source: EcoCyc

protein binding involved in protein folding

Inferred from direct assay PubMed 10380927. Source: EcoCyc

unfolded protein binding

Inferred from direct assay PubMed 9145101. Source: EcoCyc

zinc ion binding

Inferred from direct assay PubMed 11985624. Source: EcoliWiki

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6 Ref.11
Chain2 – 638637Chaperone protein DnaK HAMAP-Rule MF_00332
PRO_0000078458

Amino acid modifications

Modified residue701N6-succinyllysine Ref.18
Modified residue1091N6-acetyllysine Ref.17
Modified residue1991Phosphothreonine; by autocatalysis Ref.12 Ref.13
Modified residue2451N6-acetyllysine; alternate Ref.17
Modified residue2451N6-succinyllysine; alternate Ref.18
Modified residue2461N6-succinyllysine Ref.18
Modified residue3041N6-acetyllysine; alternate Ref.17
Modified residue3041N6-succinyllysine; alternate Ref.18
Modified residue3591N6-succinyllysine Ref.18
Modified residue4211N6-acetyllysine Ref.17
Modified residue5021N6-succinyllysine Ref.18
Modified residue5281N6-succinyllysine Ref.18
Modified residue5561N6-acetyllysine Ref.17
Modified residue5871N6-succinyllysine Ref.18

Experimental info

Mutagenesis321G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. Ref.9 Ref.10
Mutagenesis4361V → I in SEG-2; confers temperature sensitivity. Ref.10
Mutagenesis4551G → D in dnaK756(TS); confers temperature sensitivity. Ref.9
Mutagenesis4681G → D in dnaK756(TS); confers temperature sensitivity. Ref.9

Secondary structure

.............................................................................................................. 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6Y8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5A8589B21D7CD9C1

FASTA63869,115
        10         20         30         40         50         60 
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT 

        70         80         90        100        110        120 
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL 

       130        140        150        160        170        180 
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG 

       190        200        210        220        230        240 
LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL 

       250        260        270        280        290        300 
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 

       310        320        330        340        350        360 
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE 

       370        380        390        400        410        420 
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT 

       430        440        450        460        470        480 
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA 

       490        500        510        520        530        540 
DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD 

       550        560        570        580        590        600 
HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 

       610        620        630 
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK 

« Hide

References

« Hide 'large scale' references
[1]"Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous."
Bardwell J.C.A., Craig E.A.
Proc. Natl. Acad. Sci. U.S.A. 81:848-852(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK."
Schmid D., Jaussi R., Christen P.
Eur. J. Biochem. 208:699-704(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[7]"Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product."
Ohki M., Tamura F., Nishimura S., Uchida H.
J. Biol. Chem. 261:1778-1781(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 590-638.
[8]"The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein."
Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C.
J. Biol. Chem. 261:1782-1785(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-638.
[9]"DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts)."
Miyazaki T., Tanaka S., Fujita H., Itikawa H.
J. Bacteriol. 174:3715-3722(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-32; GLY-455 AND GLY-468.
Strain: B.
[10]"Involvement of DnaK protein in mini-F plasmid replication: temperature-sensitive seg mutations are located in the dnaK gene."
Ezaki B., Ogura T., Mori H., Niki H., Hiraga S.
Mol. Gen. Genet. 218:183-189(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-32 AND VAL-436.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]"Identification of phosphoproteins in Escherichia coli."
Freestone P., Grant S., Toth I., Norris V.
Mol. Microbiol. 15:573-580(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, PROTEIN SEQUENCE OF 2-11.
[12]"DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity."
McCarty J.S., Walker G.C.
Proc. Natl. Acad. Sci. U.S.A. 88:9513-9517(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-199.
[13]"Inhibition of DnaK autophosphorylation by heat shock proteins and polypeptide substrates."
Panagiotidis C.A., Burkholder W.F., Gaitanaris G.A., Gragerov A., Gottesman M.E., Silverstein S.J.
J. Biol. Chem. 269:16643-16647(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-199.
[14]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[15]"In vivo analysis of the overlapping functions of DnaK and trigger factor."
Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U., Georgopoulos C.
EMBO Rep. 5:195-200(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[16]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[17]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304; LYS-421 AND LYS-556, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[18]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-70; LYS-245; LYS-246; LYS-304; LYS-359; LYS-502; LYS-528 AND LYS-587.
Strain: K12.
[19]"Structural analysis of substrate binding by the molecular chaperone DnaK."
Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M., Gottesman M.E., Hendrickson W.A.
Science 272:1606-1614(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 389-607.
[20]"NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction."
Wang H., Kurochkin A.V., Pang Y., Hu W., Flynn G.C., Zuiderweg E.R.P.
Biochemistry 37:7929-7940(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-562.
[21]"Structural insights into substrate binding by the molecular chaperone DnaK."
Pellecchia M., Montgomery D.L., Stevens S.Y., Vander Kooi C.W., Feng H.P., Gierasch L.M., Zuiderweg E.R.P.
Nat. Struct. Biol. 7:298-303(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 394-508.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01298 Genomic DNA. Translation: AAA23694.1.
U00096 Genomic DNA. Translation: AAC73125.1.
AP009048 Genomic DNA. Translation: BAB96589.1.
D10765 Genomic DNA. Translation: BAA01595.1.
M12565 Genomic DNA. Translation: AAA23692.1.
PIRIQECDK. A03311.
RefSeqNP_414555.1. NC_000913.3.
YP_488320.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BPRNMR-A386-561[»]
1DG4NMR-A393-507[»]
1DKGX-ray2.80D1-383[»]
1DKXX-ray2.00A389-607[»]
1DKYX-ray2.80A/B389-607[»]
1DKZX-ray2.00A389-607[»]
1Q5LNMR-A393-506[»]
2BPRNMR-A386-561[»]
2KHONMR-A1-605[»]
3DPOX-ray2.10A/B389-607[»]
3DPPX-ray2.50A/B389-607[»]
3DPQX-ray2.60A/B/E/F389-607[»]
3QNJX-ray2.28A/B389-607[»]
4B9QX-ray2.40A/B/C/D1-605[»]
4E81X-ray1.90A/B389-607[»]
4EZNX-ray1.80A/B389-607[»]
4EZOX-ray1.90A/B389-607[»]
4EZPX-ray1.65A/B389-607[»]
4EZQX-ray2.00A389-607[»]
4EZRX-ray1.90A389-607[»]
4EZSX-ray1.90A389-607[»]
4EZTX-ray2.00A389-607[»]
4EZUX-ray1.90A389-607[»]
4EZVX-ray2.10A/B389-607[»]
4EZWX-ray1.80A/B/C/D389-607[»]
4EZXX-ray1.70A/B389-607[»]
4EZYX-ray1.85A389-607[»]
4EZZX-ray2.05A389-607[»]
4F00X-ray1.95A389-607[»]
4F01X-ray1.40A/B389-607[»]
4HY9X-ray1.55A/B389-607[»]
4HYBX-ray1.70A/B389-607[»]
4JN4X-ray2.30A/B2-610[»]
4JNEX-ray1.96A/B2-610[»]
4JNFX-ray1.62A389-610[»]
4JWCX-ray1.80A/B389-607[»]
4JWDX-ray1.95A/B389-607[»]
4JWEX-ray1.95A/B389-607[»]
4JWIX-ray1.90A/B389-607[»]
ProteinModelPortalP0A6Y8.
SMRP0A6Y8. Positions 4-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid849153. 7 interactions.
DIPDIP-35751N.
IntActP0A6Y8. 369 interactions.
MINTMINT-7259066.
STRING511145.b0014.

Protein family/group databases

TCDB1.A.33.1.2. the cation channel-forming heat shock protein-70 (hsp70) family.

PTM databases

PhosSiteP010484.

2D gel databases

SWISS-2DPAGEP0A6Y8.

Proteomic databases

PaxDbP0A6Y8.
PRIDEP0A6Y8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73125; AAC73125; b0014.
BAB96589; BAB96589; BAB96589.
GeneID12930526.
944750.
KEGGecj:Y75_p0014.
eco:b0014.
PATRIC32115121. VBIEscCol129921_0012.

Organism-specific databases

EchoBASEEB0237.
EcoGeneEG10241. dnaK.

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228136.
KOK04043.
OMAMITKNTT.
OrthoDBEOG6JMMSV.
PhylomeDBP0A6Y8.
ProtClustDBPRK00290.

Enzyme and pathway databases

BioCycEcoCyc:EG10241-MONOMER.
ECOL316407:JW0013-MONOMER.

Gene expression databases

GenevestigatorP0A6Y8.

Family and domain databases

HAMAPMF_00332. DnaK.
InterProIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
TIGRFAMsTIGR02350. prok_dnaK. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6Y8.
PROP0A6Y8.

Entry information

Entry nameDNAK_ECOLI
AccessionPrimary (citable) accession number: P0A6Y8
Secondary accession number(s): P04475
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene