ID   DNAK_GEOSE              Reviewed;         608 AA.
AC   Q45551;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
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   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NUB36;
RX   PubMed=8621094; DOI=10.1016/0378-1119(95)00859-4;
RA   Herbort M., Schoen U., Lang J., Schumann W.;
RT   "Cloning and sequencing of the dnaK operon of Bacillus
RT   stearothermophilus.";
RL   Gene 170:81-84(1996).
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; X90709; CAA62239.1; -; Genomic_DNA.
DR   PIR; JC4738; JC4738.
DR   AlphaFoldDB; Q45551; -.
DR   SMR; Q45551; -.
DR   PRIDE; Q45551; -.
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..608
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078419"
FT   REGION          576..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         172
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  66311 MW;  16A865A1939B52A2 CRC64;
     MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGNRTTPSVV AFKNGERLVG EVAKRQAITN
     PNTVISIKRH MGTDYKVEIE GKKYTPQEIS AIILQYLKSY AEDYLGEPVT RAVITVPAYF
     NDAQRQATKD AGRIAGLEVE RIINEPTAAA LAYGLDKEED QTILVYDLGG GTFDVSILEL
     GDGVFEVKAT AGDNHLGGDD FDQVIIDYLV DQFKQEHGID LSKDKMALQR LKDAAEKAKK
     ELSGVTQTQI SLPFISANEN GPLHLETTLT RAKFEELFAH LVERTMGPVR QALQDAGLTP
     EDIDKIILVG GSTRIPAVQE AIKRELGKEP HKGVNPDEVV AIGAAIQGGV IAGEVKDVVL
     LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQIFTTAAD NQTTVDIHVL QGERPMAADN
     KTLGRFQLTG YPPAPRGVPQ IEVTFDIDAN GIVHVRAKDL GTNKEQSITI KSSSGLSEEE
     IQRMIKEAEE NAEADRKRKE AAELRNEADQ LIFTTEKTLK EVEGKVDEAE VKKAREAKDA
     LKAALEKNDL DEIRKKKEAL QEAVQQLSIK LYEQAAKQAQ NQQAGADGAT KKDDNIVDAE
     FEEVKDDK