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P0A6Y8

- DNAK_ECOLI

UniProt

P0A6Y8 - DNAK_ECOLI

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Protein

Chaperone protein DnaK

Gene

dnaK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.

GO - Molecular functioni

  1. ADP binding Source: EcoCyc
  2. ATP binding Source: EcoCyc
  3. protein binding involved in protein folding Source: EcoCyc
  4. unfolded protein binding Source: EcoCyc
  5. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. cellular response to unfolded protein Source: EcoCyc
  2. chaperone cofactor-dependent protein refolding Source: EcoCyc
  3. chaperone mediated protein folding requiring cofactor Source: EcoCyc
  4. DNA replication Source: UniProtKB-KW
  5. protein complex assembly Source: EcoCyc
  6. protein complex disassembly Source: EcoCyc
  7. protein unfolding Source: EcoCyc
  8. response to heat Source: EcoCyc
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 1 Publication. Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
  3. plasma membrane Source: UniProtKB-KW
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 identifierActions
Mutagenesisi32 – 321G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. 2 Publications
Mutagenesisi436 – 4361V → I in SEG-2; confers temperature sensitivity. 1 Publication
Mutagenesisi455 – 4551G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication
Mutagenesisi468 – 4681G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 638637Chaperone protein DnaKPRO_0000078458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-succinyllysine1 Publication
Modified residuei109 – 1091N6-acetyllysine1 Publication
Modified residuei199 – 1991Phosphothreonine; by autocatalysis2 Publications
Modified residuei245 – 2451N6-acetyllysine; alternate1 Publication
Modified residuei245 – 2451N6-succinyllysine; alternate1 Publication
Modified residuei246 – 2461N6-succinyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysine; alternate1 Publication
Modified residuei304 – 3041N6-succinyllysine; alternate1 Publication
Modified residuei359 – 3591N6-succinyllysine1 Publication
Modified residuei421 – 4211N6-acetyllysine1 Publication
Modified residuei502 – 5021N6-succinyllysine1 Publication
Modified residuei528 – 5281N6-succinyllysine1 Publication
Modified residuei556 – 5561N6-acetyllysine1 Publication
Modified residuei587 – 5871N6-succinyllysine1 Publication

Post-translational modificationi

Autophosphorylated; GrpE inhibits the autophosphorylation.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A6Y8.
PRIDEiP0A6Y8.

2D gel databases

SWISS-2DPAGEP0A6Y8.

PTM databases

PhosSiteiP010484.

Expressioni

Gene expression databases

GenevestigatoriP0A6Y8.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
aspAP0AC382EBI-542092,EBI-544200
cbpAP366594EBI-542092,EBI-546131
dnaJP086225EBI-542092,EBI-545285
fabFP0AAI52EBI-542092,EBI-542783
fbaAP0AB712EBI-542092,EBI-370916
gloAP0AC812EBI-542092,EBI-551143
htpGP0A6Z33EBI-542092,EBI-369221
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

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi11 – 2010Combined sources
Beta strandi23 – 264Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 424Combined sources
Beta strandi48 – 514Combined sources
Helixi52 – 565Combined sources
Helixi57 – 604Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 673Combined sources
Helixi69 – 713Combined sources
Turni72 – 743Combined sources
Beta strandi76 – 794Combined sources
Helixi80 – 889Combined sources
Beta strandi90 – 956Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 13120Combined sources
Beta strandi137 – 1426Combined sources
Helixi148 – 16013Combined sources
Beta strandi164 – 1707Combined sources
Helixi171 – 18111Combined sources
Beta strandi187 – 1959Combined sources
Beta strandi200 – 21011Combined sources
Beta strandi213 – 22412Combined sources
Helixi229 – 24820Combined sources
Helixi252 – 2543Combined sources
Helixi256 – 27217Combined sources
Turni273 – 2753Combined sources
Beta strandi276 – 28914Combined sources
Beta strandi292 – 30110Combined sources
Helixi302 – 32726Combined sources
Helixi331 – 3333Combined sources
Beta strandi335 – 3417Combined sources
Helixi342 – 3454Combined sources
Helixi347 – 35711Combined sources
Beta strandi363 – 3653Combined sources
Turni367 – 3693Combined sources
Helixi370 – 38213Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi392 – 3954Combined sources
Beta strandi399 – 4035Combined sources
Turni404 – 4063Combined sources
Beta strandi407 – 4126Combined sources
Beta strandi414 – 4163Combined sources
Beta strandi417 – 43014Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi436 – 4449Combined sources
Beta strandi445 – 4473Combined sources
Helixi448 – 4503Combined sources
Beta strandi451 – 4599Combined sources
Helixi466 – 4683Combined sources
Beta strandi472 – 4787Combined sources
Beta strandi480 – 4823Combined sources
Beta strandi484 – 4907Combined sources
Turni491 – 4933Combined sources
Beta strandi496 – 5005Combined sources
Helixi503 – 5053Combined sources
Helixi509 – 52113Combined sources
Helixi523 – 55331Combined sources
Helixi554 – 5563Combined sources
Helixi559 – 57719Combined sources
Helixi581 – 59414Combined sources
Helixi596 – 6005Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BPRNMR-A384-561[»]
1DG4NMR-A393-507[»]
1DKGX-ray2.80D1-383[»]
1DKXX-ray2.00A389-607[»]
1DKYX-ray2.80A/B389-607[»]
1DKZX-ray2.00A389-607[»]
1Q5LNMR-A393-507[»]
2BPRNMR-A384-561[»]
2KHONMR-A1-605[»]
3DPOX-ray2.10A/B389-607[»]
3DPPX-ray2.50A/B389-607[»]
3DPQX-ray2.60A/B/E/F389-601[»]
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[»]
4R5GX-ray3.45A/B389-607[»]
4R5IX-ray1.97A389-607[»]
4R5JX-ray2.36A/B/C/D389-607[»]
4R5KX-ray1.75A/B389-607[»]
4R5LX-ray2.97A/B/C/D389-607[»]
ProteinModelPortaliP0A6Y8.
SMRiP0A6Y8. Positions 4-604.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6Y8.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000228136.
InParanoidiP0A6Y8.
KOiK04043.
OMAiQRDVAIM.
OrthoDBiEOG6JMMSV.
PhylomeDBiP0A6Y8.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
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]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV
60 70 80 90 100
GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD
110 120 130 140 150
AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ
160 170 180 190 200
RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF
210 220 230 240 250
DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI
260 270 280 290 300
DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
310 320 330 340 350
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ
360 370 380 390 400
KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG
410 420 430 440 450
IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD
460 470 480 490 500
NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT
510 520 530 540 550
IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV
560 570 580 590 600
EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME
610 620 630
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
Length:638
Mass (Da):69,115
Last modified:January 23, 2007 - v2
Checksum:i5A8589B21D7CD9C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiA03311. IQECDK.
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:
EMBLi
GenBanki
DDBJi
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 A03311. IQECDK.
RefSeqi NP_414555.1. NC_000913.3.
YP_488320.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BPR NMR - A 384-561 [» ]
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 393-507 [» ]
2BPR NMR - A 384-561 [» ]
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 389-601 [» ]
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 [» ]
4R5G X-ray 3.45 A/B 389-607 [» ]
4R5I X-ray 1.97 A 389-607 [» ]
4R5J X-ray 2.36 A/B/C/D 389-607 [» ]
4R5K X-ray 1.75 A/B 389-607 [» ]
4R5L X-ray 2.97 A/B/C/D 389-607 [» ]
ProteinModelPortali P0A6Y8.
SMRi P0A6Y8. Positions 4-604.
ModBasei Search...
MobiDBi 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-2DPAGE 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.
InParanoidi P0A6Y8.
KOi K04043.
OMAi QRDVAIM.
OrthoDBi EOG6JMMSV.
PhylomeDBi P0A6Y8.

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

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPi MF_00332. DnaK.
InterProi IPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
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' publications
  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. 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. 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. Cited for: STRUCTURE BY NMR OF 394-508.

Entry informationi

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: November 26, 2014
This is version 110 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3