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P0A6Y8

- DNAK_ECOLI

UniProt

P0A6Y8 - DNAK_ECOLI

Protein

Chaperone protein DnaK

Gene

dnaK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 Source: IntAct
    4. protein binding involved in protein folding Source: EcoCyc
    5. unfolded protein binding Source: EcoCyc
    6. 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

    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-SubCell

    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 autocatalysis3 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 – 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-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[»]
    ProteinModelPortaliP0A6Y8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6Y8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    HOGENOMiHOG000228136.
    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

    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.
    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:
    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 A03311. IQECDK.
    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 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 [» ]
    ProteinModelPortali P0A6Y8.
    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.
    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

    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: October 1, 2014
    This is version 108 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