Gene Details


gene name: dnaK


locus tag k12ECK0014 Crenarchaeota Euryarchaeota Nanoarcheota Alphaproteobacteria Betaproteobacteria Gammaproteobacteria Deltaproteobacteria Epsilonproteobacteria Cyanobacteria Actinobacteridae Firmicutes Spirochaetes others Protist Microsporidia Fungi Metazoa Plantae
information on phylogenetic profile
locus tag mg1655b0014
locus tag w3110JW0013
gene name k12dnaK
locus namednaK
synonyms of locus namegrpF, seg, lop, groPAB, groPC, groPF, grpC

scop id53067
superfamilyActin-like ATPase domain
pfam idPF00012
pfam domainHsp70 protein
TIGRFAMno information

swissprot nameDNAK_ECOLI
descriptionChaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa|protein) (HSP70).
seq length637
fastaseq

go idGO:0005737; GO:0006457; GO:0006970
go termcytoplasm; protein folding; response to osmotic stress

gene product descriptionchaperone Hsp70, co-chaperone with DnaJ
comment gene product description
evidenceE
context
gene product descFactor
cell locationCytoplasmic
featuresCDS

functional category codeO
functional categoryPosttranslational modification, protein turnover, chaperones

reference #1Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system.

Maki J., Southworth D., Culver G. (RNA. 2003 Dec; 9(12):1418-21)
reference #2Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed.

Agashe V., Guha S., Chang H., Genevaux P., Hayer-Hartl M., Stemp M., Georgopoulos C., Hartl F., Barral J. (Cell. 2004 Apr 16; 117(2):199-209)
reference #3DNA ligase: structure, mechanism, and function.

Lehman I. (Science. 1974 Nov 29; 186(4166):790-7)
reference #4Heat shock regulation of sigmaS turnover: a role for DnaK and relationship between stress responses mediated by sigmaS and sigma32 in Escherichia coli.

Muffler A., Barth M., Marschall C., Hengge-Aronis R. (J Bacteriol. 1997 Jan; 179(2):445-52)
reference #5Enhanced deletion formation by aberrant DNA replication in Escherichia coli.

Saveson C., Lovett S. (Genetics. 1997 Jun; 146(2):457-70)
reference #6Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

Langer T., Lu C., Echols H., Flanagan J., Hayer M., Hartl F. (Nature. 1992 Apr 23; 356(6371):683-9)
reference #7Relative expression of the products of glyoxylate bypass operon: contributions of transcription and translation.

Chung T., Resnik E., Stueland C., LaPorte D. (J Bacteriol. 1993 Jul; 175(14):4572-5)
reference #8The 70-kDa heat-shock protein/DnaK chaperone system is required for the productive folding of ribulose-biphosphate carboxylase subunits in Escherichia coli.

Checa S., Viale A. (Eur J Biochem. 1997 Sep 15; 248(3):848-55)
reference #9DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

Schröder H., Langer T., Hartl F., Bukau B. (EMBO J. 1993 Nov; 12(11):4137-44)
reference #10Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.

Hesterkamp T., Bukau B. (EMBO J. 1998 Aug 17; 17(16):4818-28)
reference #11Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.

Davis J., Voisine C., Craig E. (Proc Natl Acad Sci U S A. 1999 Aug 3; 96(16):9269-76)
reference #12Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

Deuerling E., Schulze-Specking A., Tomoyasu T., Mogk A., Bukau B. (Nature. 1999 Aug 12; 400(6745):693-6)
reference #13Structural insights into substrate binding by the molecular chaperone DnaK.

Pellecchia M., Montgomery D., Stevens S., Vander Kooi C., Feng H., Gierasch L., Zuiderweg E. (Nat Struct Biol. 2000 Apr; 7(4):298-303)
reference #14Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK.

Schmid D., Jaussi R., Christen P. (Eur J Biochem. 1992 Sep 15; 208(3):699-704)
reference #15DNA 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. 1992 Jun; 174(11):3715-22)
reference #16DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.

McCarty J., Walker G. (Proc Natl Acad Sci U S A. 1991 Nov 1; 88(21):9513-7)
reference #17Involvement 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. 1989 Aug; 218(2):183-9)
reference #18Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.

Ohki M., Tamura F., Nishimura S., Uchida H. (J Biol Chem. 1986 Feb 5; 261(4):1778-81)
reference #19The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.

Bardwell J., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C. (J Biol Chem. 1986 Feb 5; 261(4):1782-5)
reference #20Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.

Bardwell J., Craig E. (Proc Natl Acad Sci U S A. 1984 Feb; 81(3):848-52)
reference #21Identification of phosphoproteins in Escherichia coli.

Freestone P., Grant S., Toth I., Norris V. (Mol Microbiol. 1995 Feb; 15(3):573-80)
reference #22Inhibition of DnaK autophosphorylation by heat shock proteins and polypeptide substrates.

Panagiotidis C., Burkholder W., Gaitanaris G., Gragerov A., Gottesman M., Silverstein S. (J Biol Chem. 1994 Jun 17; 269(24):16643-7)
reference #23Structural analysis of substrate binding by the molecular chaperone DnaK.

Zhu X., Zhao X., Burkholder W., Gragerov A., Ogata C., Gottesman M., Hendrickson W. (Science. 1996 Jun 14; 272(5268):1606-14)
reference #24Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.

Link A., Robison K., Church G. (Electrophoresis. 1997 Aug; 18(8):1259-313)
reference #25NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.

Wang H., Kurochkin A., Pang Y., Hu W., Flynn G., Zuiderweg E. (Biochemistry. 1998 Jun 2; 37(22):7929-40)

phylogenetic profile
 
1 1 1 1 1 572 602 1 1 64 634 639 582 1 1 1 554 561 1 611
613 601 611 605 623 622 621 623 635 635 619 616 626 596 596 791 792 793 791 816
816 772 811 787 781 778 780 795 744 873 872 871 881 881 877 848 847 872 877 664
642 649 649 637 657 669 672 724 751 729 778 662 662 669 671 665 622 622 624 647
633 628 678 659 671 617 620 603 617 628 631 631 631 631 545 552 530 530 558 596
545 528 619 587 636 636 636 636 636 609 609 602 605 607 608 608 608 608 608 663
520 828 989 959 978 989 867 1049 1138 1138 1138 918 863 863 1007 836 1020 1050 926 914
894 1109 1109 1109 945 1136 1136 989 970 980 941 872 872 853 855 1062 1062 1062 630 712
714 661 661 661 678 678 669 706 571 658 703 645 708 578 615 717 682 706 704 682
694 687 689 692 545 685 655 676 696 727 724 710 709 709 549 717 755 695 675