ID   DNAK_BACC7              Reviewed;         611 AA.
AC   B7HPL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=BCAH187_A4447;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) 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; CP001177; ACJ82033.1; -; Genomic_DNA.
DR   RefSeq; WP_000034690.1; NC_011658.1.
DR   AlphaFoldDB; B7HPL3; -.
DR   SMR; B7HPL3; -.
DR   EnsemblBacteria; ACJ82033; ACJ82033; BCAH187_A4447.
DR   GeneID; 59155114; -.
DR   GeneID; 64199659; -.
DR   KEGG; bcr:BCAH187_A4447; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002214; 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..611
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119668"
FT   REGION          579..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   611 AA;  65821 MW;  1BAAF8B3EAB87C9A CRC64;
     MSKIIGIDLG TTNSCVAVME GGEPKVIPNP EGNRTTPSVV AFKNEERQVG EVAKRQAITN
     PNTIMSVKRH MGTDYKVEIE GKEYTPQEIS AIILQNLKAS AEAYLGETVT KAVITVPAYF
     NDAERQATKD AGRIAGLEVE RIINEPTAAA LAYGLEKQDE EQKILVYDLG GGTFDVSILE
     LADGTFEVIS TAGDNRLGGD DFDQVIIDHL VAEFKKENNI DLSQDKMALQ RLKDAAEKAK
     KDLSGVTQTQ ISLPFISAGA AGPLHLELTL TRAKFEELSA NLVERTLEPT RRALKDAGLS
     ASELDRVILV GGSTRIPAVQ EAIKRETGKE PYKGVNPDEV VALGAAVQGG VLTGDVEGVL
     LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMSAD
     NKTLGRFQLT DIPPAPRGIP QIEVTFDIDA NGIVNVRAKD LGTSKEQAIT IQSSSGLSDE
     EVDRMVKEAE ANADADQKRK EEVELRNEAD QLVFQTDKVV KDLEGKVDAA EVAKATEAKE
     ALQAAIEKNE LEEIRAKKDA LQEIVQQLTV KLYEQAQAAA GQAEGAQGAQ DAGAKKDNVV
     DAEFEEVKED K