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P0A6Y8

- DNAK_ECOLI

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Protein
Chaperone protein DnaK
Gene
dnaK, groP, grpF, seg, b0014, JW0013

Gene:

dnaK, groP, grpF, seg, b0014, JW0013
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P0A6Y8 - DNAK_ECOLI

Protein:

Chaperone protein DnaK
Protein Existence: Experimental evidence at protein level

Functioni

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.UniRule annotation

GO - Molecular functioni

  1. ADP bindingInferred from direct assayi PubMed 19439666PubMed 7776367 Source: EcoCyc
  2. ATP bindingInferred from direct assayi PubMed 7776367 Source: EcoCyc
  3. protein binding involved in protein foldingInferred from direct assayi PubMed 10380927 Source: EcoCyc
  4. unfolded protein bindingInferred from direct assayi PubMed 9145101 Source: EcoCyc
  5. zinc ion bindingInferred from direct assayi PubMed 11985624 Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. ADP bindingInferred from direct assayi PubMed 19439666PubMed 7776367 Source: EcoCyc
  2. ATP bindingInferred from direct assayi PubMed 7776367 Source: EcoCyc
  3. protein binding involved in protein foldingInferred from direct assayi PubMed 10380927 Source: EcoCyc
  4. unfolded protein bindingInferred from direct assayi PubMed 9145101 Source: EcoCyc
  5. zinc ion bindingInferred from direct assayi PubMed 11985624 Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

DNA replication, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10241-MONOMER.
ECOL316407:JW0013-MONOMER.

Protein family/group databases

TCDBi1.A.33.1.2. the cation channel-forming heat shock protein-70 (hsp70) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein DnaK
Alternative name(s):
HSP70
Heat shock 70 kDa protein
Heat shock protein 70
Gene namesi
Name:dnaK
Synonyms:groP, grpF, seg
Ordered Locus Names:b0014, JW0013
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10241. dnaK.

Subcellular locationi

Cytoplasm. Cell inner membrane; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasmInferred from direct assayi PubMed 16858726 Source: UniProtKB
  2. membraneInferred from direct assayi PubMed 16858726 Source: UniProtKB
  3. plasma membraneInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Mutagenesisi321G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. 2 Publications
Mutagenesisi4361V → I in SEG-2; confers temperature sensitivity. 1 Publication
Mutagenesisi4551G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication
Mutagenesisi4681G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Initiator methioninei11Removed3 Publications
Chaini2 – 638637Chaperone protein DnaKUniRule annotation
PRO_0000078458

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei701N6-succinyllysine1 Publication
Modified residuei1091N6-acetyllysine1 Publication
Modified residuei1991Phosphothreonine; by autocatalysis2 Publications
Modified residuei2451N6-acetyllysine; alternate1 Publication
Modified residuei2451N6-succinyllysine; alternate1 Publication
Modified residuei2461N6-succinyllysine1 Publication
Modified residuei3041N6-acetyllysine; alternate1 Publication
Modified residuei3041N6-succinyllysine; alternate1 Publication
Modified residuei3591N6-succinyllysine1 Publication
Modified residuei4211N6-acetyllysine1 Publication
Modified residuei5021N6-succinyllysine1 Publication
Modified residuei5281N6-succinyllysine1 Publication
Modified residuei5561N6-acetyllysine1 Publication
Modified residuei5871N6-succinyllysine1 Publication

Post-translational modificationi

Autophosphorylated; GrpE inhibits the autophosphorylation.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A6Y8.
PRIDEiP0A6Y8.

2D gel databases

SWISS-2DPAGEiP0A6Y8.

PTM databases

PhosSiteiP010484.

Expressioni

Gene expression databases

GenevestigatoriP0A6Y8.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
aspAP0AC382EBI-542092,EBI-544200
dnaJP086225EBI-542092,EBI-545285
fabFP0AAI52EBI-542092,EBI-542783
fbaAP0AB712EBI-542092,EBI-370916
gloAP0AC812EBI-542092,EBI-551143
rneP215139EBI-542092,EBI-549958
ydhRP0ACX32EBI-542092,EBI-544817
ygcPQ469062EBI-542092,EBI-557727

Protein-protein interaction databases

BioGridi849153. 7 interactions.
DIPiDIP-35751N.
IntActiP0A6Y8. 369 interactions.
MINTiMINT-7259066.
STRINGi511145.b0014.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi4 – 85
Beta strandi11 – 2010
Beta strandi23 – 264
Beta strandi34 – 374
Beta strandi39 – 424
Beta strandi48 – 514
Helixi52 – 565
Helixi57 – 604
Helixi62 – 643
Beta strandi65 – 673
Helixi69 – 713
Turni72 – 743
Beta strandi76 – 794
Helixi80 – 889
Beta strandi90 – 956
Beta strandi99 – 1057
Beta strandi108 – 1103
Helixi112 – 13120
Beta strandi137 – 1426
Helixi148 – 16013
Beta strandi164 – 1707
Helixi171 – 18111
Beta strandi187 – 1959
Beta strandi200 – 21011
Beta strandi213 – 22412
Helixi229 – 24820
Helixi252 – 2543
Helixi256 – 27217
Turni273 – 2753
Beta strandi276 – 28914
Beta strandi292 – 30110
Helixi302 – 32726
Helixi331 – 3333
Beta strandi335 – 3417
Helixi342 – 3454
Helixi347 – 35711
Beta strandi363 – 3653
Turni367 – 3693
Helixi370 – 38213
Beta strandi384 – 3863
Beta strandi392 – 3954
Beta strandi399 – 4035
Turni404 – 4063
Beta strandi407 – 4126
Beta strandi414 – 4163
Beta strandi417 – 43014
Beta strandi432 – 4343
Beta strandi436 – 4449
Beta strandi445 – 4473
Helixi448 – 4503
Beta strandi451 – 4599
Helixi466 – 4683
Beta strandi472 – 4787
Beta strandi480 – 4823
Beta strandi484 – 4907
Turni491 – 4933
Beta strandi496 – 5005
Helixi503 – 5053
Helixi509 – 52113
Helixi523 – 55331
Helixi554 – 5563
Helixi559 – 57719
Helixi581 – 59414
Helixi596 – 6005

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A6Y8.
SMRiP0A6Y8. Positions 4-604.

Miscellaneous databases

EvolutionaryTraceiP0A6Y8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000228136.
KOiK04043.
OMAiMITKNTT.
OrthoDBiEOG6JMMSV.
ProtClustDBiPRK00290.

Family and domain databases

HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6Y8-1 [UniParc]FASTA

« Hide

MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV    50
GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD 100
AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ 150
RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF 200
DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI 250
DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 300
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ 350
KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG 400
IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD 450
NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT 500
IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV 550
EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 600
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK 638
Length:638
Mass (Da):69,115
Last modified:January 23, 2007 - v2
Checksum:i5A8589B21D7CD9C1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiIQECDK. A03311.
RefSeqiNP_414555.1. NC_000913.3.
YP_488320.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73125; AAC73125; b0014.
BAB96589; BAB96589; BAB96589.
GeneIDi12930526.
944750.
KEGGiecj:Y75_p0014.
eco:b0014.
PATRICi32115121. VBIEscCol129921_0012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi IQECDK. A03311.
RefSeqi NP_414555.1. NC_000913.3.
YP_488320.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BPR NMR - A 386-561 [» ]
1DG4 NMR - A 393-507 [» ]
1DKG X-ray 2.80 D 1-383 [» ]
1DKX X-ray 2.00 A 389-607 [» ]
1DKY X-ray 2.80 A/B 389-607 [» ]
1DKZ X-ray 2.00 A 389-607 [» ]
1Q5L NMR - A 393-506 [» ]
2BPR NMR - A 386-561 [» ]
2KHO NMR - A 1-605 [» ]
3DPO X-ray 2.10 A/B 389-607 [» ]
3DPP X-ray 2.50 A/B 389-607 [» ]
3DPQ X-ray 2.60 A/B/E/F 389-607 [» ]
3QNJ X-ray 2.28 A/B 389-607 [» ]
4B9Q X-ray 2.40 A/B/C/D 1-605 [» ]
4E81 X-ray 1.90 A/B 389-607 [» ]
4EZN X-ray 1.80 A/B 389-607 [» ]
4EZO X-ray 1.90 A/B 389-607 [» ]
4EZP X-ray 1.65 A/B 389-607 [» ]
4EZQ X-ray 2.00 A 389-607 [» ]
4EZR X-ray 1.90 A 389-607 [» ]
4EZS X-ray 1.90 A 389-607 [» ]
4EZT X-ray 2.00 A 389-607 [» ]
4EZU X-ray 1.90 A 389-607 [» ]
4EZV X-ray 2.10 A/B 389-607 [» ]
4EZW X-ray 1.80 A/B/C/D 389-607 [» ]
4EZX X-ray 1.70 A/B 389-607 [» ]
4EZY X-ray 1.85 A 389-607 [» ]
4EZZ X-ray 2.05 A 389-607 [» ]
4F00 X-ray 1.95 A 389-607 [» ]
4F01 X-ray 1.40 A/B 389-607 [» ]
4HY9 X-ray 1.55 A/B 389-607 [» ]
4HYB X-ray 1.70 A/B 389-607 [» ]
4JN4 X-ray 2.30 A/B 2-610 [» ]
4JNE X-ray 1.96 A/B 2-610 [» ]
4JNF X-ray 1.62 A 389-610 [» ]
4JWC X-ray 1.80 A/B 389-607 [» ]
4JWD X-ray 1.95 A/B 389-607 [» ]
4JWE X-ray 1.95 A/B 389-607 [» ]
4JWI X-ray 1.90 A/B 389-607 [» ]
ProteinModelPortali P0A6Y8.
SMRi P0A6Y8. Positions 4-604.
ModBasei Search...

Protein-protein interaction databases

BioGridi 849153. 7 interactions.
DIPi DIP-35751N.
IntActi P0A6Y8. 369 interactions.
MINTi MINT-7259066.
STRINGi 511145.b0014.

Protein family/group databases

TCDBi 1.A.33.1.2. the cation channel-forming heat shock protein-70 (hsp70) family.

PTM databases

PhosSitei P010484.

2D gel databases

SWISS-2DPAGEi P0A6Y8.

Proteomic databases

PaxDbi P0A6Y8.
PRIDEi P0A6Y8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73125 ; AAC73125 ; b0014 .
BAB96589 ; BAB96589 ; BAB96589 .
GeneIDi 12930526.
944750.
KEGGi ecj:Y75_p0014.
eco:b0014.
PATRICi 32115121. VBIEscCol129921_0012.

Organism-specific databases

EchoBASEi EB0237.
EcoGenei EG10241. dnaK.

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000228136.
KOi K04043.
OMAi MITKNTT.
OrthoDBi EOG6JMMSV.
ProtClustDBi PRK00290.

Enzyme and pathway databases

BioCyci EcoCyc:EG10241-MONOMER.
ECOL316407:JW0013-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6Y8.
PROi P0A6Y8.

Gene expression databases

Genevestigatori P0A6Y8.

Family and domain databases

HAMAPi MF_00332. DnaK.
InterProi IPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
TIGRFAMsi TIGR02350. prok_dnaK. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  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, 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.

Entry nameiDNAK_ECOLI
AccessioniPrimary (citable) accession number: P0A6Y8
Secondary accession number(s): P04475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

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