ID   DNAK_DEIDV              Reviewed;         628 AA.
AC   C1CZH9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Deide_21970;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO47227.1; -; Genomic_DNA.
DR   RefSeq; WP_012694348.1; NC_012526.1.
DR   AlphaFoldDB; C1CZH9; -.
DR   SMR; C1CZH9; -.
DR   STRING; 546414.Deide_21970; -.
DR   PaxDb; C1CZH9; -.
DR   EnsemblBacteria; ACO47227; ACO47227; Deide_21970.
DR   KEGG; ddr:Deide_21970; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002208; 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; 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; 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; 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..628
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205182"
FT   REGION          545..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..611
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   628 AA;  67796 MW;  10A521F53E9CBFBE CRC64;
     MAKAVGIDLG TTNSVISVME GGRPEVIVNA EGGRTTPSVV AYKGDERLVG QIARRQAALN
     PAATLFEVKR FIGRRWDEVK EEAARSPFKV KEGPGGSVRI EVNGQDLAPE QVSAEVLRKL
     VSDASAKLGQ KITDAVITVP AYFDNSQREA TKQAGEIAGL NVLRVINEPT AAALAYGLER
     KGNETVLVFD LGGGTFDVTI LELGDGVFEV KSTAGDTHLG GADFDHRIVD WLAEEFNREH
     NFDLRKDKQA LQRLIEAAEK AKIDLSNASE SSISLPFITF DPETRTPMHL ERTLSRAKFE
     ELTADLLRRV RKPVEQALAD AKLSASDIDE VILVGGSTRI PAVKRIVQDL VGKTPNESVN
     PDEAVALGAA VQAGIIQGDS ALGDIVLVDV TPLTLGVEVK GGMIAPMITR NTTVPAKKTE
     IYTTAENNQP GVEINVLQGE RPMASDNKSL GRFKLEGIPP MRAGQAQIEV TFDIDANGIL
     HVTAKEKTSG KEASIRIENT TTLDKSDVER MVREAEENAA ADKLRREKVE KRNNLDSLRV
     QATQQLEENE GAAQDAKDAL KAAADEAEEA VRSEDDARIE SAQKRLEEEL RTFMTAQQAA
     GQGQPQGAQA QGTKADDDVI DADFKAAE