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Protein

Chaperone protein DnaK

Gene

dnaK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

  • ADP binding Source: EcoCyc
  • ATP binding Source: EcoCyc
  • protein binding involved in protein folding Source: EcoCyc
  • sigma factor antagonist activity Source: EcoCyc
  • unfolded protein binding Source: EcoCyc
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • cellular response to unfolded protein Source: EcoCyc
  • chaperone cofactor-dependent protein refolding Source: EcoCyc
  • chaperone mediated protein folding requiring cofactor Source: EcoCyc
  • DNA replication Source: UniProtKB-KW
  • protein complex assembly Source: EcoCyc
  • protein complex disassembly Source: EcoCyc
  • 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.
MetaCyc:EG10241-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10241. dnaK.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
  • plasma membrane 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)DescriptionActionsGraphical viewLength
Mutagenesisi32G → D in SEG-1 and dnaK756(TS); confers temperature sensitivity. 2 Publications1
Mutagenesisi436V → I in SEG-2; confers temperature sensitivity. 1 Publication1
Mutagenesisi455G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication1
Mutagenesisi468G → D in dnaK756(TS); confers temperature sensitivity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000784582 – 638Chaperone protein DnaKAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei70N6-succinyllysine1 Publication1
Modified residuei109N6-acetyllysine1 Publication1
Modified residuei199Phosphothreonine; by autocatalysis2 Publications1
Modified residuei245N6-acetyllysine; alternate1 Publication1
Modified residuei245N6-succinyllysine; alternate1 Publication1
Modified residuei246N6-succinyllysine1 Publication1
Modified residuei304N6-acetyllysine; alternate1 Publication1
Modified residuei304N6-succinyllysine; alternate1 Publication1
Modified residuei359N6-succinyllysine1 Publication1
Modified residuei421N6-acetyllysine1 Publication1
Modified residuei502N6-succinyllysine1 Publication1
Modified residuei528N6-succinyllysine1 Publication1
Modified residuei556N6-acetyllysine1 Publication1
Modified residuei587N6-succinyllysine1 Publication1

Post-translational modificationi

Autophosphorylated; GrpE inhibits the autophosphorylation.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP0A6Y8.
PaxDbiP0A6Y8.
PRIDEiP0A6Y8.

2D gel databases

SWISS-2DPAGEP0A6Y8.

PTM databases

iPTMnetiP0A6Y8.

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
rpoHP0AGB35EBI-542092,EBI-555342
ydhRP0ACX32EBI-542092,EBI-544817
ygcPQ469062EBI-542092,EBI-557727

GO - Molecular functioni

  • protein binding involved in protein folding Source: EcoCyc
  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259520. 125 interactors.
849153. 8 interactors.
DIPiDIP-35751N.
IntActiP0A6Y8. 369 interactors.
MINTiMINT-7259066.
STRINGi511145.b0014.

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi11 – 20Combined sources10
Beta strandi23 – 26Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi39 – 42Combined sources4
Beta strandi48 – 51Combined sources4
Helixi52 – 56Combined sources5
Helixi57 – 60Combined sources4
Helixi62 – 64Combined sources3
Beta strandi65 – 67Combined sources3
Helixi69 – 71Combined sources3
Turni72 – 74Combined sources3
Beta strandi76 – 79Combined sources4
Helixi80 – 88Combined sources9
Beta strandi90 – 95Combined sources6
Beta strandi99 – 105Combined sources7
Beta strandi108 – 110Combined sources3
Helixi112 – 131Combined sources20
Beta strandi137 – 142Combined sources6
Helixi148 – 160Combined sources13
Beta strandi164 – 170Combined sources7
Helixi171 – 181Combined sources11
Beta strandi187 – 195Combined sources9
Beta strandi200 – 210Combined sources11
Beta strandi213 – 224Combined sources12
Helixi229 – 248Combined sources20
Helixi252 – 254Combined sources3
Helixi256 – 272Combined sources17
Turni273 – 275Combined sources3
Beta strandi276 – 289Combined sources14
Beta strandi292 – 301Combined sources10
Helixi302 – 327Combined sources26
Helixi331 – 333Combined sources3
Beta strandi335 – 341Combined sources7
Helixi342 – 345Combined sources4
Helixi347 – 357Combined sources11
Beta strandi363 – 365Combined sources3
Turni367 – 369Combined sources3
Helixi370 – 382Combined sources13
Beta strandi384 – 386Combined sources3
Beta strandi392 – 395Combined sources4
Beta strandi399 – 403Combined sources5
Turni404 – 406Combined sources3
Beta strandi407 – 412Combined sources6
Beta strandi414 – 416Combined sources3
Beta strandi417 – 430Combined sources14
Beta strandi432 – 434Combined sources3
Beta strandi436 – 444Combined sources9
Beta strandi445 – 447Combined sources3
Helixi448 – 450Combined sources3
Beta strandi451 – 459Combined sources9
Helixi466 – 468Combined sources3
Beta strandi472 – 478Combined sources7
Beta strandi480 – 482Combined sources3
Beta strandi484 – 490Combined sources7
Turni491 – 493Combined sources3
Beta strandi496 – 500Combined sources5
Helixi503 – 505Combined sources3
Helixi509 – 521Combined sources13
Helixi523 – 553Combined sources31
Helixi554 – 556Combined sources3
Helixi559 – 577Combined sources19
Helixi581 – 594Combined sources14
Helixi596 – 600Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6Y8.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiENOG4105CFG. Bacteria.
COG0443. LUCA.
HOGENOMiHOG000228136.
InParanoidiP0A6Y8.
KOiK04043.
OMAiEKMAPPQ.
PhylomeDBiP0A6Y8.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK. 1 hit.
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.
WP_000516135.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73125; AAC73125; b0014.
BAB96589; BAB96589; BAB96589.
GeneIDi944750.
KEGGiecj:JW0013.
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.
PIRiA03311. IQECDK.
RefSeqiNP_414555.1. NC_000913.3.
WP_000516135.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259520. 125 interactors.
849153. 8 interactors.
DIPiDIP-35751N.
IntActiP0A6Y8. 369 interactors.
MINTiMINT-7259066.
STRINGi511145.b0014.

Protein family/group databases

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

PTM databases

iPTMnetiP0A6Y8.

2D gel databases

SWISS-2DPAGEP0A6Y8.

Proteomic databases

EPDiP0A6Y8.
PaxDbiP0A6Y8.
PRIDEiP0A6Y8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73125; AAC73125; b0014.
BAB96589; BAB96589; BAB96589.
GeneIDi944750.
KEGGiecj:JW0013.
eco:b0014.
PATRICi32115121. VBIEscCol129921_0012.

Organism-specific databases

EchoBASEiEB0237.
EcoGeneiEG10241. dnaK.

Phylogenomic databases

eggNOGiENOG4105CFG. Bacteria.
COG0443. LUCA.
HOGENOMiHOG000228136.
InParanoidiP0A6Y8.
KOiK04043.
OMAiEKMAPPQ.
PhylomeDBiP0A6Y8.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6Y8.
PROiP0A6Y8.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.