MG1655
W3110
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Gene Report : dnaK
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)
Acta Microbiol Pol. 1997;46(1):7-17.
Escherichia coli defects caused by null mutations in dnaK and dnaJ genes.
Paciorek J, Kardys K, Lobacz B, Wolska KI. ( 9271843 )
     Deletion OCR27 (D)  ,  OCR27-6 (D)  ,  OCR27-7 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  dnaK
Related strains
     Strains Search Search strains by gene name:  dnaK   Search strains by all related name:  dnaK b0014 ECK0014 gro groP groPAB groPC groPF grpC grpF JW0013 seg

General information  (Go to Linear View:)
 Gene Name dnaK  
 Alternative name b0014,ECK0014,gro,groP,groPAB,groPC,groPF,grpC,grpF,JW0013,seg  
 Location, Length 12,163 - 14,079 (  +  ) ;   0.26 min ; 1917 (bp) ,   638 (aa) Go to Linear View
 Product chaperone Hsp70, co-chaperone with DnaJ  
 Operon Name dnaK-tpke11-dnaJ  
 Note chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006457 - protein folding; GO_process: GO:0006970 - response to osmotic stress  
 Function factor; Chaperones,2.3.4 information transfer; protein related; chaperoning, folding,5.5.1 cell processes; adaptation to stress; osmotic pressure,7.1 location of gene products; cytoplasm  
 Gene Ontology GO:0000166 ; nucleotide binding ( dnaK )
GO:0005515 ; protein binding ( dnaK )
GO:0005524 ; ATP binding ( dnaK )
GO:0005737 ; cytoplasm ( dnaK )
GO:0005886 ; plasma membrane ( dnaK )
GO:0006260 ; DNA replication ( dnaK )
GO:0006457 ; protein folding ( dnaK )
GO:0006950 ; response to stress ( dnaK )
GO:0016020 ; membrane ( dnaK )
GO:0051082 ; unfolded protein binding ( dnaK )
 PID 1786196  
 EC number
  (KEGG Pathway)
 
 
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene dnaK ( EG10241 )  
    Number of removed 1 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) DNAB_ECOLI ( P03005 )
    -  Protein name Replicative DNA helicase  
    -  Synonyms EC 3.6.1.-  
    -  Gene name OrderedLocusNames=b4052, SF4154, S3577;  
    -  Comments
  • FUNCTION:Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with dnaC protein, primase, and other prepriming proteins.
  • SUBUNIT:Homohexamer.
  • SIMILARITY:Belongs to the helicase family. DnaB subfamily.  
  •   botton Entry name(Acc.no) DNAK_ECOLI ( P04475 )
        -  Protein name Chaperone protein dnaK  
        -  Synonyms Heat shock protein 70, Heat shock 70 kDa protein, HSP70  
        -  Gene name OrderedLocusNames=b0014, c0019, z0014, ECs0014;  
        -  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.
  • PTM:Autophosphorylated; grpE inhibits the autophosphorylation.
  • MISCELLANEOUS:The mutants dnaK756(Ts), seg-1 and seg-2 confer temperature sensitivity.
  • SIMILARITY:Belongs to the heat shock protein 70 family.  
  •   botton Entry name(Acc.no) DNAJ_ECOLI ( P08622 )
        -  Protein name Chaperone protein dnaJ  
        -  Synonyms Heat shock protein J, HSP40  
        -  Gene name Name=dnaJ; Synonyms=groP; OrderedLocusNames=b0015;  
        -  Comments
  • FUNCTION:Interacts with dnaK to disassemble a protein complex at the phage lambda origin of replication. Stimulates, jointly with grpE, the ATPase activity of dnaK.
  • COFACTOR:Binds 2 zinc ions per monomer.
  • SUBUNIT:Homodimer.
  • SUBCELLULAR LOCATION:Cytoplasmic.
  • INDUCTION:By heat shock under the control of the htpR regulatory protein.
  • SIMILARITY:Belongs to the dnaJ family.
  • SIMILARITY:Contains 1 CR domain.
  • SIMILARITY:Contains 1 J domain.  

  •  Linear View (Whole Mode)
    View Location
       0.0  –  25.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP dnaK (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Crystal Structure Of Bovine Hsc70  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70)  
             PSI-BLAST Chaperone protein dnaK2
        nr     (database updated : 2007.02.20 )
             BLAST molecular chaperone DnaK [Escherichia coli O157:H7 EDL933]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    AMIDATION    HSP70_1    HSP70_2    HSP70_3     

    Other Cross-Reference
        COG COG0443O 
        EcoCyc dnaK 

    MMBR References
    Microbiology 1996;142:2595-2602
    Defect in export and synthesis of the periplasmic galactose receptor MglB in dnaK mutants of Escherichia coli, and decreased stability of the mglB mRNA.
    el Yaagoubi, A., M. Kohiyama, and G. Richarme.
    Mol Gen Genet. 1990;223(3):361-8.
    Possible involvement of the ugpA gene product in the stable maintenance of mini-F plasmid in Escherichia coli.
    Ezaki B, Mori H, Ogura T, Hiraga S. ( 2270076 )
    Mol Gen Genet. 1989;218(2):183-9.
    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. ( 2674651 )
    J Biol Chem. 1990;265:19244-19248
    Aggregated dnaA protein is dissociated and activated for DNA replication by phospholipase or dnaK protein.
    Hwang, D. S., E. Crooke, and A. Kornberg.
    J Bacteriol. 1994;176:5648-5653
    Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma32 in Escherichia coli.
    Kanemori, M., H. Mori, and T. Yura.
    Proc Natl Acad Sci U S A. 1984;81:848-852
    Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.
    Bardwell, J. C., and E. A. Craig.
    J Bacteriol. 1994;176:764-780
    DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation.
    McCarty, J. S., and G. C. Walker.
    J Bacteriol. 1997;179:445-452
    Heat shock regulation of sigma S turnover: a role for DnaK and relationship between stress responses mediated by sigma S and sigma 32 in Escherichia coli.
    Muffler, A., M. Barth, C. Marschall, and R. Hengge-Aronis.
    Eur J Biochem. 1996;240:78-82
    Nucleotide binding to the heat-shock protein DnaK as studied by ESR spectroscopy.
    Neuhofen, S., H. Theyssen, J. Reinstein, W. E. Trommer, and P. D. Vogel.
    Biochim Biophys Acta. 1989;1009(1):94-8.
    A complete deletion mutant of the Escherichia coli dnaKdnaJ operon.
    Ohki R, Morita R, Kawamata T, Uchida H, Ohki M. ( 2675977 )
    J Bacteriol. 1987;169(1):283-90.
    Escherichia coli dnaK null mutants are inviable at high temperature.
    Paek KH, Walker GC. ( 3025174 )
    J Bacteriol. 1998;180:846-854
    Roles of DnaK and RpoS in starvation-induced thermotolerance of Escherichia coli.
    Rockabrand, D., K. Livers, T. Austin, R. Kaiser, D. Jensen, R. Burgess, and P. Blum.
    J Bacteriol. 1988;170(2):972-9.
    The dnaK gene of Escherichia coli functions in initiation of chromosome replication.
    Sakakibara Y. ( 2962992 )
    Genes Dev. 1990;4:2202-2209
    DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.
    Straus, D., W. Walter, and C. A. Gross.
    Proc Natl Acad Sci U S A. 1996;93:10632-10637
    Mutations in the C-terminal fragment of DnaK affecting peptide binding.
    Burkholder, W. F., X. Zhao, X. Zhu, W. A. Hendrickson, A. Gragerov, and M. E. Gottesman.

    Sequences
    Amino acid
    FASTA format
    0001 MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK 
    0071 RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI 
    0141 TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF DISIIEIDEV 
    0211 DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD 
    0281 VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ 
    0351 KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT 
    0421 KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD 
    0491 KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV EEAGDKLPAD 
    0561 DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME IAQQQHAQQQ TAGADASANN AKDDDVVDAE 
    0631 FEEVKDKK
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             GTCTGCAAAA AAATGAAATT GGGCAGTTGA 
    -070 AACCAGACGT TTCGCCCCTA TTACAGACTC ACAACCACAT GATGACCGAA TATATAGTGG AGACGTTTAG 
    0001 atgggtaaaa taattggtat cgacctgggt actaccaact cttgtgtagc gattatggat ggcaccactc 
    0071 ctcgcgtgct ggagaacgcc gaaggcgatc gcaccacgcc ttctatcatt gcctataccc aggatggtga 
    0141 aactctagtt ggtcagccgg ctaaacgtca ggcagtgacg aacccgcaaa acactctgtt tgcgattaaa 
    0211 cgcctgattg gtcgccgctt ccaggacgaa gaagtacagc gtgatgtttc catcatgccg ttcaaaatta 
    0281 ttgctgctga taacggcgac gcatgggtcg aagttaaagg ccagaaaatg gcaccgccgc agatttctgc 
    0351 tgaagtgctg aaaaaaatga agaaaaccgc tgaagattac ctgggtgaac cggtaactga agctgttatc 
    0421 accgtaccgg catactttaa cgatgctcag cgtcaggcaa ccaaagacgc aggccgtatc gctggtctgg 
    0491 aagtaaaacg tatcatcaac gaaccgaccg cagctgcgct ggcttacggt ctggacaaag gcactggcaa 
    0561 ccgtactatc gcggtttatg acctgggtgg tggtactttc gatatttcta ttatcgaaat cgacgaagtt 
    0631 gacggcgaaa aaaccttcga agttctggca accaacggtg atacccacct ggggggtgaa gacttcgaca 
    0701 gccgtctgat caactatctg gttgaagaat tcaagaaaga tcagggcatt gacctgcgca acgatccgct 
    0771 ggcaatgcag cgcctgaaag aagcggcaga aaaagcgaaa atcgaactgt cttccgctca gcagaccgac 
    0841 gttaacctgc catacatcac tgcagacgcg accggtccga aacacatgaa catcaaagtg actcgtgcga 
    0911 aactggaaag cctggttgaa gatctggtaa accgttccat tgagccgctg aaagttgcac tgcaggacgc 
    0981 tggcctgtcc gtatctgata tcgacgacgt tatcctcgtt ggtggtcaga ctcgtatgcc aatggttcag 
    1051 aagaaagttg ctgagttctt tggtaaagag ccgcgtaaag acgttaaccc ggacgaagct gtagcaatcg 
    1121 gtgctgctgt tcagggtggt gttctgactg gtgacgtaaa agacgtactg ctgctggacg ttaccccgct 
    1191 gtctctgggt atcgaaacca tgggcggtgt gatgacgacg ctgatcgcga aaaacaccac tatcccgacc 
    1261 aagcacagcc aggtgttctc taccgctgaa gacaaccagt ctgcggtaac catccatgtg ctgcagggtg 
    1331 aacgtaaacg tgcggctgat aacaaatctc tgggtcagtt caacctagat ggtatcaacc cggcaccgcg 
    1401 cggcatgccg cagatcgaag ttaccttcga tatcgatgct gacggtatcc tgcacgtttc cgcgaaagat 
    1471 aaaaacagcg gtaaagagca gaagatcacc atcaaggctt cttctggtct gaacgaagat gaaatccaga 
    1541 aaatggtacg cgacgcagaa gctaacgccg aagctgaccg taagtttgaa gagctggtac agactcgcaa 
    1611 ccagggcgac catctgctgc acagcacccg taagcaggtt gaagaagcag gcgacaaact gccggctgac 
    1681 gacaaaactg ctatcgagtc tgcgctgact gcactggaaa ctgctctgaa aggtgaagac aaagccgcta 
    1751 tcgaagcgaa aatgcaggaa ctggcacagg tttcccagaa actgatggaa atcgcccagc agcaacatgc 
    1821 ccagcagcag actgccggtg ctgatgcttc tgcaaacaac gcgaaagatg acgatgttgt cgacgctgaa 
    1891 tttgaagaag tcaaagacaa aaaataaTCG CCCTATAAAC GGGTAATTAT ACTGACACGG GCGAAGGGGA 
    1961 ATTTCCTCTC CGCCCGTGCA TTCATCTAGG GGCAATTTAA AAAAGATGGC TAAGCAA