ID   DNAK_DEIGD              Reviewed;         629 AA.
AC   Q1IWL4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Dgeo_2076;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; CP000359; ABF46370.1; -; Genomic_DNA.
DR   RefSeq; WP_011531196.1; NC_008025.1.
DR   AlphaFoldDB; Q1IWL4; -.
DR   SMR; Q1IWL4; -.
DR   STRING; 319795.Dgeo_2076; -.
DR   PRIDE; Q1IWL4; -.
DR   EnsemblBacteria; ABF46370; ABF46370; Dgeo_2076.
DR   KEGG; dge:Dgeo_2076; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..629
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059549"
FT   REGION          514..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         195
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   629 AA;  68368 MW;  62253CDE3DEEAFB2 CRC64;
     MPKAVGIDLG TTNSVIATME GGRPEVIVNA EGARTTPSVV AYKGDERLVG QIARRQAALN
     PKATLFEVKR FIGRRWDEVK EEAARMPFTV KEGPGGSVRI EVNGKDLAPE QVSAEVLRKL
     VADASAKLGE KITDAVITVP AYFDNSQREA TKQAGEIAGL NVLRVINEPT AAALAYGLER
     KGNETVLVFD LGGGTFDVTI LELGEGVFEV RSTAGDTHLG GADFDQRIVN WLAEEFRKEH
     NFDLRKDPQA LQRLIEAAER AKIELSNASE TTISLPFITF DPETRTPLHL ERTLSRAKFE
     ELTADLLRRV RQPVEQALAD AKLSASDIDE VILVGGSTRI PAVKRIVKEI TGKEPNESVN
     PDEAVALGAA VQAGIIQGDA NLGDIVLVDV TPLTLGVEVK GGMVAPMIPR NTTIPAKKTE
     IYTTAENNQP GVEIVVLQGE RPMAADNKSL GRFKLEGIPP MPAGRPQIEV TFDIDANGIL
     HVTAKEKTSG KEASIRIENT TTLDKSDVER MVKEAEQNAE ADRKRRERVE KRNNLDSLRV
     QALGQLEENQ SAPQDAKDRL KAAADEAEEA VRSDDDSRIE RAQKQLEEAM RSFMTAAQSG
     SQNQAGQGAQ TQTGRQEDDV IDADFKPAE