ID   DNAK_ALKCK              Reviewed;         611 AA.
AC   Q5WHG1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=ABC1659;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD64194.1; -; Genomic_DNA.
DR   RefSeq; WP_011246503.1; NC_006582.1.
DR   AlphaFoldDB; Q5WHG1; -.
DR   SMR; Q5WHG1; -.
DR   STRING; 66692.ABC1659; -.
DR   PRIDE; Q5WHG1; -.
DR   EnsemblBacteria; BAD64194; BAD64194; ABC1659.
DR   KEGG; bcl:ABC1659; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001168; 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   Reference proteome; Stress response.
FT   CHAIN           1..611
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225933"
FT   REGION          575..611
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   611 AA;  65669 MW;  07C532DE284F2ADE CRC64;
     MSKIIGIDLG TTNSCVAVME GGEATVIPNP EGNRTTPSVV AFKDGERLVG EVAKRQAITN
     PNTVISIKRH MGTDYKVDIE GKSYSPQEIS AIILQKLKAD AEAYLGEKVT KAVITVPAYF
     NDSQRQATKD AGKIAGLEVD RIVNEPTAAA LAYGLEKEDD QTILVYDLGG GTFDVSILEL
     GDGFFEVKAT SGDNKLGGDD FDEVIMDHLV AEFKKENGID LSQDKMAMQR LKDAAEKAKK
     DLSGVTQTQI SLPFITADAT GPKHLELTLT RAKFDELSAD LVERTLGPTR RALSDAGLSA
     SDIDKVVLVG GSTRIPAVQE AIKKLTGKDP HKGVNPDEVV ALGAAVQAGV LTGDVKDVVL
     LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQVFSTAAD NQPSVDIHVL QGEREMAADN
     KTLGRFQLTD IPPAPRGVPQ IEVTFDIDAN GIVNVKAKDL GTNKEQSITI TSSSGLSEEE
     IDKMVQEAEA NAEADKKRRE QVELRNEADQ LVFSTEKTLK DLGDNVDQAE KDKAEAAKDK
     LKKALEADNT DDIKAAKDEL QEIVTALTTK LYEQAAQAAQ AQQDGGNESA DKQDDNVVDA
     DYEEVNDDDK K