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Reviewed, UniProtKB/Swiss-Prot P0A6Y8 (DNAK_ECOLI)

Last modified July 7, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chaperone protein dnaK
Alternative name(s):
    Heat shock protein 70
    Heat shock 70 kDa protein
    HSP70
Gene names
Name: dnaK
Synonyms: groP, grpF, seg
Ordered Locus Names: b0014, JW0013
OrganismEscherichia coli (strain K12) [Complete 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 MF_00332

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein. Ref.14

Post-translational modification

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

Sequence similarities

Belongs to the heat shock protein 70 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11 Ref.5 Ref.6
Chain2 – 638637Chaperone protein dnaK HAMAP MF_00332
PRO_0000078458

Amino acid modifications

Modified residue1091N6-acetyllysine Ref.15
Modified residue1991Phosphothreonine; by autocatalysis Ref.12 Ref.13
Modified residue2451N6-acetyllysine Ref.15
Modified residue3041N6-acetyllysine Ref.15
Modified residue4211N6-acetyllysine Ref.15
Modified residue5561N6-acetyllysine Ref.15

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6Y8-1 [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: 6322174] [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: 1630901] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 1396676] [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: 9298646] [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: 3003084] [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: 3003085] [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: 1592823] [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: 2674651] [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: 7783627] [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: 1835085] [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: 8206983] [Abstract]
Cited for: PHOSPHORYLATION AT THR-199.
[14]"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: 16079137] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[15]"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: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304; LYS-421 AND LYS-556, MASS SPECTROMETRY.
[16]"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: 8658133] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 389-607.
[17]"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: 9609686] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-562.
[18]"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: 10742174] [Abstract]
Cited for: STRUCTURE BY NMR OF 394-508.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_000678.1.
NP_414555.1.

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0A6Y8. 365 interactions.

Protein family/group databases

TCDB1.A.33.1.2. cation channel-forming heat shock protein-70 (Hsp70) family.

PTM databases

PhosSiteP0A6Y8.

2-D gel databases

SWISS-2DPAGEP0A6Y8.
2DBase-EcoliP0A6Y8.
ECO2DBASEB066.0. 6TH EDITION.

Genome annotation databases

GeneID944750.
GenomeReviewsGene locus JW0013 in contig AP009048_GR.
Gene locus b0014 in contig U00096_GR.
KEGGecj:JW0013.
eco:b0014.

Organism-specific databases

EchoBASEEB0237.
EcoGeneEG10241. dnaK.
CMRSearch...

Phylogenomic databases

HOGENOMP0A6Y8.
OMAP0A6Y8. ANNGDAW.

Enzyme and pathway databases

BioCycEcoCyc:EG10241-MON.

Family and domain databases

HAMAPMF_00332.
[Tree]
InterProIPR012725. DnaK_prok.
IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]
PANTHERPTHR19375. Hsp70. 1 hit.
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
ProDomPD000089. Hsp70. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR02350. prok_dnaK. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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: July 7, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents