DNAK_ECOLI
ID DNAK_ECOLI Reviewed; 638 AA.
AC P0A6Y8; P04475;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; Synonyms=groP, grpF, seg; OrderedLocusNames=b0014, JW0013;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6322174; DOI=10.1073/pnas.81.3.848;
RA Bardwell J.C.A., Craig E.A.;
RT "Major heat shock gene of Drosophila and the Escherichia coli heat-
RT inducible dnaK gene are homologous.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:848-852(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=1396676; DOI=10.1111/j.1432-1033.1992.tb17237.x;
RA Schmid D., Jaussi R., Christen P.;
RT "Precursor of mitochondrial aspartate aminotransferase synthesized in
RT Escherichia coli is complexed with heat-shock protein DnaK.";
RL Eur. J. Biochem. 208:699-704(1992).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 590-638.
RX PubMed=3003084; DOI=10.1016/s0021-9258(17)36007-6;
RA Ohki M., Tamura F., Nishimura S., Uchida H.;
RT "Nucleotide sequence of the Escherichia coli dnaJ gene and purification of
RT the gene product.";
RL J. Biol. Chem. 261:1778-1781(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-638.
RX PubMed=3003085; DOI=10.1016/s0021-9258(17)36008-8;
RA Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C.;
RT "The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene
RT that encodes a heat shock protein.";
RL J. Biol. Chem. 261:1782-1785(1986).
RN [9]
RP MUTAGENESIS OF GLY-32; GLY-455 AND GLY-468.
RC STRAIN=B;
RX PubMed=1592823; DOI=10.1128/jb.174.11.3715-3722.1992;
RA Miyazaki T., Tanaka S., Fujita H., Itikawa H.;
RT "DNA sequence analysis of the dnaK gene of Escherichia coli B and of two
RT dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and
RT dnaK756(Ts).";
RL J. Bacteriol. 174:3715-3722(1992).
RN [10]
RP MUTAGENESIS OF GLY-32 AND VAL-436.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2674651; DOI=10.1007/bf00331267;
RA Ezaki B., Ogura T., Mori H., Niki H., Hiraga S.;
RT "Involvement of DnaK protein in mini-F plasmid replication: temperature-
RT sensitive seg mutations are located in the dnaK gene.";
RL Mol. Gen. Genet. 218:183-189(1989).
RN [11]
RP PHOSPHORYLATION, AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=7783627; DOI=10.1111/j.1365-2958.1995.tb02270.x;
RA Freestone P., Grant S., Toth I., Norris V.;
RT "Identification of phosphoproteins in Escherichia coli.";
RL Mol. Microbiol. 15:573-580(1995).
RN [12]
RP PHOSPHORYLATION AT THR-199.
RX PubMed=1835085; DOI=10.1073/pnas.88.21.9513;
RA McCarty J.S., Walker G.C.;
RT "DnaK as a thermometer: threonine-199 is site of autophosphorylation and is
RT critical for ATPase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9513-9517(1991).
RN [13]
RP PHOSPHORYLATION AT THR-199.
RX PubMed=8206983; DOI=10.1016/s0021-9258(19)89438-3;
RA Panagiotidis C.A., Burkholder W.F., Gaitanaris G.A., Gragerov A.,
RA Gottesman M.E., Silverstein S.J.;
RT "Inhibition of DnaK autophosphorylation by heat shock proteins and
RT polypeptide substrates.";
RL J. Biol. Chem. 269:16643-16647(1994).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14726952; DOI=10.1038/sj.embor.7400067;
RA Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U.,
RA Georgopoulos C.;
RT "In vivo analysis of the overlapping functions of DnaK and trigger
RT factor.";
RL EMBO Rep. 5:195-200(2004).
RN [16]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304; LYS-421
RP AND LYS-556, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [18]
RP SUCCINYLATION AT LYS-70; LYS-245; LYS-246; LYS-304; LYS-359; LYS-502;
RP LYS-528 AND LYS-587.
RC STRAIN=K12;
RX PubMed=21151122; DOI=10.1038/nchembio.495;
RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT "Identification of lysine succinylation as a new post-translational
RT modification.";
RL Nat. Chem. Biol. 7:58-63(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 389-607.
RX PubMed=8658133; DOI=10.1126/science.272.5268.1606;
RA Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M., Gottesman M.E.,
RA Hendrickson W.A.;
RT "Structural analysis of substrate binding by the molecular chaperone
RT DnaK.";
RL Science 272:1606-1614(1996).
RN [20]
RP STRUCTURE BY NMR OF 387-562.
RX PubMed=9609686; DOI=10.1021/bi9800855;
RA Wang H., Kurochkin A.V., Pang Y., Hu W., Flynn G.C., Zuiderweg E.R.P.;
RT "NMR solution structure of the 21 kDa chaperone protein DnaK substrate
RT binding domain: a preview of chaperone-protein interaction.";
RL Biochemistry 37:7929-7940(1998).
RN [21]
RP STRUCTURE BY NMR OF 394-508.
RX PubMed=10742174; DOI=10.1038/74062;
RA Pellecchia M., Montgomery D.L., Stevens S.Y., Vander Kooi C.W., Feng H.P.,
RA Gierasch L.M., Zuiderweg E.R.P.;
RT "Structural insights into substrate binding by the molecular chaperone
RT DnaK.";
RL Nat. Struct. Biol. 7:298-303(2000).
CC -!- FUNCTION: Plays an essential role in the initiation of phage lambda DNA
CC replication, where it acts in an ATP-dependent fashion with the DnaJ
CC protein to release lambda O and P proteins from the preprimosomal
CC complex. DnaK is also involved in chromosomal DNA replication, possibly
CC through an analogous interaction with the DnaA protein. Also
CC participates actively in the response to hyperosmotic shock.
CC -!- INTERACTION:
CC P0A6Y8; P0AC38: aspA; NbExp=3; IntAct=EBI-542092, EBI-544200;
CC P0A6Y8; P36659: cbpA; NbExp=5; IntAct=EBI-542092, EBI-546131;
CC P0A6Y8; P63284: clpB; NbExp=8; IntAct=EBI-542092, EBI-546182;
CC P0A6Y8; P08622: dnaJ; NbExp=8; IntAct=EBI-542092, EBI-545285;
CC P0A6Y8; P0AAI5: fabF; NbExp=3; IntAct=EBI-542092, EBI-542783;
CC P0A6Y8; P0AB71: fbaA; NbExp=3; IntAct=EBI-542092, EBI-370916;
CC P0A6Y8; P0AC81: gloA; NbExp=3; IntAct=EBI-542092, EBI-551143;
CC P0A6Y8; P09372: grpE; NbExp=10; IntAct=EBI-542092, EBI-547441;
CC P0A6Y8; P0A6Z3: htpG; NbExp=3; IntAct=EBI-542092, EBI-369221;
CC P0A6Y8; P45578: luxS; NbExp=2; IntAct=EBI-542092, EBI-562313;
CC P0A6Y8; P12282: moeB; NbExp=2; IntAct=EBI-542092, EBI-554435;
CC P0A6Y8; P69924: nrdB; NbExp=2; IntAct=EBI-542092, EBI-555196;
CC P0A6Y8; P28304: qorA; NbExp=2; IntAct=EBI-542092, EBI-556687;
CC P0A6Y8; P21513: rne; NbExp=10; IntAct=EBI-542092, EBI-549958;
CC P0A6Y8; P0AGB3: rpoH; NbExp=7; IntAct=EBI-542092, EBI-555342;
CC P0A6Y8; P0ADX9: rsmD; NbExp=2; IntAct=EBI-542092, EBI-561207;
CC P0A6Y8; P23721: serC; NbExp=2; IntAct=EBI-542092, EBI-557952;
CC P0A6Y8; P0A853: tnaA; NbExp=2; IntAct=EBI-542092, EBI-371316;
CC P0A6Y8; P0ACX3: ydhR; NbExp=3; IntAct=EBI-542092, EBI-544817;
CC P0A6Y8; Q46906: ygcP; NbExp=3; IntAct=EBI-542092, EBI-557727;
CC P0A6Y8; P37342: yjjI; NbExp=2; IntAct=EBI-542092, EBI-548519;
CC P0A6Y8; P04233: CD74; Xeno; NbExp=8; IntAct=EBI-542092, EBI-2622890;
CC P0A6Y8; A0A0G4PYZ0: HLA-DRB1; Xeno; NbExp=7; IntAct=EBI-542092, EBI-25339717;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell
CC inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16079137}.
CC -!- PTM: Autophosphorylated; GrpE inhibits the autophosphorylation.
CC {ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:7783627,
CC ECO:0000269|PubMed:8206983}.
CC -!- DISRUPTION PHENOTYPE: Non-essential; synthetic lethality is seen in a
CC triple tig-dnaK-dnaJ disruption, although this depends on temperature
CC (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at
CC all at 43 degrees) and strain background.
CC {ECO:0000269|PubMed:14726952}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; K01298; AAA23694.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73125.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96589.1; -; Genomic_DNA.
DR EMBL; D10765; BAA01595.1; -; Genomic_DNA.
DR EMBL; M12565; AAA23692.1; -; Genomic_DNA.
DR PIR; A03311; IQECDK.
DR RefSeq; NP_414555.1; NC_000913.3.
DR RefSeq; WP_000516135.1; NZ_SSZK01000015.1.
DR PDB; 1BPR; NMR; -; A=384-561.
DR PDB; 1DG4; NMR; -; A=393-507.
DR PDB; 1DKG; X-ray; 2.80 A; D=1-383.
DR PDB; 1DKX; X-ray; 2.00 A; A=389-607.
DR PDB; 1DKY; X-ray; 2.80 A; A/B=389-607.
DR PDB; 1DKZ; X-ray; 2.00 A; A=389-607.
DR PDB; 1Q5L; NMR; -; A=393-507.
DR PDB; 2BPR; NMR; -; A=384-561.
DR PDB; 2KHO; NMR; -; A=1-605.
DR PDB; 3DPO; X-ray; 2.10 A; A/B=389-607.
DR PDB; 3DPP; X-ray; 2.50 A; A/B=389-607.
DR PDB; 3DPQ; X-ray; 2.60 A; A/B/E/F=389-601.
DR PDB; 3QNJ; X-ray; 2.28 A; A/B=389-607.
DR PDB; 4B9Q; X-ray; 2.40 A; A/B/C/D=1-605.
DR PDB; 4E81; X-ray; 1.90 A; A/B=389-607.
DR PDB; 4EZN; X-ray; 1.80 A; A/B=389-607.
DR PDB; 4EZO; X-ray; 1.90 A; A/B=389-607.
DR PDB; 4EZP; X-ray; 1.65 A; A/B=389-607.
DR PDB; 4EZQ; X-ray; 2.00 A; A=389-607.
DR PDB; 4EZR; X-ray; 1.90 A; A=389-607.
DR PDB; 4EZS; X-ray; 1.90 A; A=389-607.
DR PDB; 4EZT; X-ray; 2.00 A; A=389-607.
DR PDB; 4EZU; X-ray; 1.90 A; A=389-607.
DR PDB; 4EZV; X-ray; 2.10 A; A/B=389-607.
DR PDB; 4EZW; X-ray; 1.80 A; A/B/C/D=389-607.
DR PDB; 4EZX; X-ray; 1.70 A; A/B=389-607.
DR PDB; 4EZY; X-ray; 1.85 A; A=389-607.
DR PDB; 4EZZ; X-ray; 2.05 A; A=389-607.
DR PDB; 4F00; X-ray; 1.95 A; A=389-607.
DR PDB; 4F01; X-ray; 1.40 A; A/B=389-607.
DR PDB; 4HY9; X-ray; 1.55 A; A/B=389-607.
DR PDB; 4HYB; X-ray; 1.70 A; A/B=389-607.
DR PDB; 4JN4; X-ray; 2.30 A; A/B=2-610.
DR PDB; 4JNE; X-ray; 1.96 A; A/B=2-610.
DR PDB; 4JNF; X-ray; 1.62 A; A=389-610.
DR PDB; 4JWC; X-ray; 1.80 A; A/B=389-607.
DR PDB; 4JWD; X-ray; 1.95 A; A/B=389-607.
DR PDB; 4JWE; X-ray; 1.95 A; A/B=389-607.
DR PDB; 4JWI; X-ray; 1.90 A; A/B=389-607.
DR PDB; 4R5G; X-ray; 3.45 A; A/B=389-607.
DR PDB; 4R5I; X-ray; 1.97 A; A=389-607.
DR PDB; 4R5J; X-ray; 2.36 A; A/B/C/D=389-607.
DR PDB; 4R5K; X-ray; 1.75 A; A/B=389-607.
DR PDB; 4R5L; X-ray; 2.97 A; A/B/C/D=389-607.
DR PDB; 5NRO; X-ray; 3.25 A; A=1-605.
DR PDB; 5OOW; X-ray; 2.90 A; A/B=183-383.
DR PDB; 7JMM; X-ray; 2.56 A; A=389-607.
DR PDB; 7JN8; X-ray; 3.09 A; A=389-607.
DR PDB; 7JN9; X-ray; 2.40 A; A=389-607.
DR PDB; 7JNE; X-ray; 2.54 A; A=389-607.
DR PDB; 7KO2; X-ray; 2.64 A; A/B/C/D=1-609.
DR PDB; 7KRT; X-ray; 2.79 A; A/B/C/D=1-600.
DR PDB; 7KRU; X-ray; 1.82 A; A/B=1-540.
DR PDB; 7KRV; X-ray; 1.92 A; A/B=1-540.
DR PDB; 7KRW; X-ray; 7.70 A; A/B/C/D=1-614.
DR PDB; 7KZI; X-ray; 2.82 A; A/B=1-609.
DR PDB; 7KZU; X-ray; 2.15 A; A=2-540.
DR PDB; 7N6J; X-ray; 2.00 A; A=389-607.
DR PDB; 7N6K; X-ray; 2.55 A; A=389-607.
DR PDB; 7N6L; X-ray; 2.40 A; A=389-607.
DR PDB; 7N6M; X-ray; 1.82 A; A=389-607.
DR PDBsum; 1BPR; -.
DR PDBsum; 1DG4; -.
DR PDBsum; 1DKG; -.
DR PDBsum; 1DKX; -.
DR PDBsum; 1DKY; -.
DR PDBsum; 1DKZ; -.
DR PDBsum; 1Q5L; -.
DR PDBsum; 2BPR; -.
DR PDBsum; 2KHO; -.
DR PDBsum; 3DPO; -.
DR PDBsum; 3DPP; -.
DR PDBsum; 3DPQ; -.
DR PDBsum; 3QNJ; -.
DR PDBsum; 4B9Q; -.
DR PDBsum; 4E81; -.
DR PDBsum; 4EZN; -.
DR PDBsum; 4EZO; -.
DR PDBsum; 4EZP; -.
DR PDBsum; 4EZQ; -.
DR PDBsum; 4EZR; -.
DR PDBsum; 4EZS; -.
DR PDBsum; 4EZT; -.
DR PDBsum; 4EZU; -.
DR PDBsum; 4EZV; -.
DR PDBsum; 4EZW; -.
DR PDBsum; 4EZX; -.
DR PDBsum; 4EZY; -.
DR PDBsum; 4EZZ; -.
DR PDBsum; 4F00; -.
DR PDBsum; 4F01; -.
DR PDBsum; 4HY9; -.
DR PDBsum; 4HYB; -.
DR PDBsum; 4JN4; -.
DR PDBsum; 4JNE; -.
DR PDBsum; 4JNF; -.
DR PDBsum; 4JWC; -.
DR PDBsum; 4JWD; -.
DR PDBsum; 4JWE; -.
DR PDBsum; 4JWI; -.
DR PDBsum; 4R5G; -.
DR PDBsum; 4R5I; -.
DR PDBsum; 4R5J; -.
DR PDBsum; 4R5K; -.
DR PDBsum; 4R5L; -.
DR PDBsum; 5NRO; -.
DR PDBsum; 5OOW; -.
DR PDBsum; 7JMM; -.
DR PDBsum; 7JN8; -.
DR PDBsum; 7JN9; -.
DR PDBsum; 7JNE; -.
DR PDBsum; 7KO2; -.
DR PDBsum; 7KRT; -.
DR PDBsum; 7KRU; -.
DR PDBsum; 7KRV; -.
DR PDBsum; 7KRW; -.
DR PDBsum; 7KZI; -.
DR PDBsum; 7KZU; -.
DR PDBsum; 7N6J; -.
DR PDBsum; 7N6K; -.
DR PDBsum; 7N6L; -.
DR PDBsum; 7N6M; -.
DR AlphaFoldDB; P0A6Y8; -.
DR SMR; P0A6Y8; -.
DR BioGRID; 4259520; 182.
DR BioGRID; 849153; 11.
DR DIP; DIP-35751N; -.
DR IntAct; P0A6Y8; 380.
DR MINT; P0A6Y8; -.
DR STRING; 511145.b0014; -.
DR TCDB; 1.A.33.1.2; the cation channel-forming heat shock protein-70 (hsp70) family.
DR CarbonylDB; P0A6Y8; -.
DR iPTMnet; P0A6Y8; -.
DR SWISS-2DPAGE; P0A6Y8; -.
DR jPOST; P0A6Y8; -.
DR PaxDb; P0A6Y8; -.
DR PRIDE; P0A6Y8; -.
DR EnsemblBacteria; AAC73125; AAC73125; b0014.
DR EnsemblBacteria; BAB96589; BAB96589; BAB96589.
DR GeneID; 67416093; -.
DR GeneID; 944750; -.
DR KEGG; ecj:JW0013; -.
DR KEGG; eco:b0014; -.
DR PATRIC; fig|1411691.4.peg.2270; -.
DR EchoBASE; EB0237; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR InParanoid; P0A6Y8; -.
DR OMA; ISIKRHM; -.
DR PhylomeDB; P0A6Y8; -.
DR BioCyc; EcoCyc:EG10241-MON; -.
DR BioCyc; MetaCyc:EG10241-MON; -.
DR EvolutionaryTrace; P0A6Y8; -.
DR PRO; PR:P0A6Y8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016234; C:inclusion body; IDA:CACAO.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:CAFA.
DR GO; GO:0044183; F:protein folding chaperone; IDA:EcoCyc.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:EcoCyc.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:CAFA.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:CAFA.
DR GO; GO:0032984; P:protein-containing complex disassembly; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IDA:EcoCyc.
DR DisProt; DP02985; -.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell inner membrane; Cell membrane;
KW Chaperone; Cytoplasm; Direct protein sequencing; DNA replication; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1396676,
FT ECO:0000269|PubMed:7783627, ECO:0000269|PubMed:9298646"
FT CHAIN 2..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078458"
FT REGION 602..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:1835085,
FT ECO:0000269|PubMed:8206983"
FT MOD_RES 245
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 245
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 246
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 304
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 304
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 359
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 502
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 528
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 556
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 587
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MUTAGEN 32
FT /note="G->D: In SEG-1 and dnaK756(TS); confers temperature
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:1592823,
FT ECO:0000269|PubMed:2674651"
FT MUTAGEN 436
FT /note="V->I: In SEG-2; confers temperature sensitivity."
FT /evidence="ECO:0000269|PubMed:2674651"
FT MUTAGEN 455
FT /note="G->D: In dnaK756(TS); confers temperature
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:1592823"
FT MUTAGEN 468
FT /note="G->D: In dnaK756(TS); confers temperature
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:1592823"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4JNE"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2KHO"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 112..131
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 229..248
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 256..272
FT /evidence="ECO:0007829|PDB:4JNE"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 276..289
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 302..327
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4JNE"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4JNE"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:7KZU"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:7KZI"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:4EZW"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:4F01"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1Q5L"
FT STRAND 417..430
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4JNE"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1Q5L"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4JNF"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:1BPR"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:4F01"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:4F01"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 523..553
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 559..577
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 581..594
FT /evidence="ECO:0007829|PDB:4F01"
FT HELIX 596..600
FT /evidence="ECO:0007829|PDB:4F01"
SQ SEQUENCE 638 AA; 69115 MW; 5A8589B21D7CD9C1 CRC64;
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD
HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
