ID   DNAK_GEOTN              Reviewed;         605 AA.
AC   A4IR31;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=GTNG_2440;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO67785.1; -; Genomic_DNA.
DR   RefSeq; WP_008879919.1; NC_009328.1.
DR   AlphaFoldDB; A4IR31; -.
DR   SMR; A4IR31; -.
DR   STRING; 420246.GTNG_2440; -.
DR   PRIDE; A4IR31; -.
DR   EnsemblBacteria; ABO67785; ABO67785; GTNG_2440.
DR   KEGG; gtn:GTNG_2440; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001578; 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; 2.
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   Stress response.
FT   CHAIN           1..605
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059568"
FT   REGION          579..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         172
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   605 AA;  65588 MW;  0ECD2C3B4BC16DC8 CRC64;
     MSKIIGIDLG TTNSCVAVLE GGEAKVIPNP EGSRTTPSVV AFKNGERLVG EVAKRQAITN
     PNTIISIKRH MGTDYKVEIE GKQYTPQEIS AIILQYLKSY AEDYLGEPVT RAVITVPAYF
     NDAQRQATKD AGRIAGLEVE RIINEPTAAA LAYGLDKGED QTILVYDLGG GTFDVSILEL
     GDGVFEVKAT AGDNHLGGDD FDQVIIDYLV SQFKQENGID LSKDKMALQR LKDAAEKAKK
     ELSGVTQTQI SLPFISANEN GPLHLETTLT RAKFEELSAH LVERTMGPVR QALQDAGLTS
     ADIDKVILVG GSTRIPAVQE AIKRELGKEP HKGVNPDEVV AIGAAIQGGV IAGEVKDIVL
     LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQVFTTAAD NQTTVDIHVL QGERPMAADN
     KTLGRFQLTD IPPAPRGVPQ IEVTFDIDAN GIVHVRAKDL GTNKEQSITI KSSSGLSEEE
     IQRMIKEAEE NAEADRKRKE AADLRNEADQ LIFTTEKTVK ELEGKVSADE IKKAQEAKDA
     LKAALEKNDL DDIRKKKDAL QEAVQQLSIK LYEQAAQQAQ QAQSGAADKK DNVVDAEFEE
     VNDDK