ID   DNAK_PARTM              Reviewed;         607 AA.
AC   Q9KWS7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 100.
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;
OS   Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=1426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43742 / DSM 2542 / NCIMB 11955 / NRRL B-14516 / KP 1006;
RX   PubMed=15188890; DOI=10.1023/a:1002483620374;
RA   Watanabe K., Iwashiro T., Suzuki Y.;
RT   "Features of dnaK operon genes of the obligate thermophile Bacillus
RT   thermoglucosidasius KP1006.";
RL   Antonie Van Leeuwenhoek 77:241-250(2000).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AB017035; BAB03215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KWS7; -.
DR   SMR; Q9KWS7; -.
DR   STRING; 1426.AOT13_16990; -.
DR   eggNOG; COG0443; Bacteria.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078422"
FT   REGION          571..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..607
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         169
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   607 AA;  66083 MW;  31F3C8509F2D69E6 CRC64;
     MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGSRTTPSVV AFKNGERLVA KRQAITNPNT
     IISIKRHMGT DYKVEIEGKK YTPQEISAII LQYLKSYAED YLGEPVTRAV ITVPAYFNDA
     QRQATKDAGR IAGLQVERII NEPTAAALAY GLDKEEDQTI LVYDLGGGTF DVSILELGDG
     VFEVKATAGD NHLGGDDFDQ VIIDYLVEQF KQEHGIDLSK DKMALQRLKD AAEKAKKELS
     GVTQTQISLP FISANETGPL HIETTLTRAK FEELSAHLVE RTMGPVRQAL QDAGLTPADI
     DKVILVGGST RIPAVQEAIK RELGKEPHKG VNPDEVVAIG AAIQGGVIAG EVKDVVLLDV
     TPLSLGIETM GGVFTKLIER NTTIPTSKSQ IFTTAADNQT TVDIHVLQGE RPMAADNKTL
     GRFQLTDIPP APRGVPQIEV TFDIDANGIV HVRAKDLGTN KEQSITIKSS SGLSEEEIQR
     MIKEAEENAE ADRKRKEAAE LRNEADHLVF TTEKTLKEVE GKVDEAEVKK AREAKDALKA
     ALEKNDIDDI RKKKEALQEI VQQLSVKLYE QAAKQAQAQQ QTGAGDAAKK DDNVVDAEFE
     EVKDDNK