ID   DNAK_BACC1              Reviewed;         611 AA.
AC   Q730M1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=BCE_4395;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43296.1; -; Genomic_DNA.
DR   RefSeq; WP_000034691.1; NC_003909.8.
DR   PRIDE; Q730M1; -.
DR   EnsemblBacteria; AAS43296; AAS43296; BCE_4395.
DR   KEGG; bca:BCE_4395; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002527; 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_0000225931"
FT   REGION          579..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..611
FT                   /note="Basic and acidic residues"
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;  65875 MW;  BA2657DD9BF6AB94 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 AXPLHLELTL 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