ID   DNAK_BACCN              Reviewed;         611 AA.
AC   A7GT08;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Bcer98_3040;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23266.1; -; Genomic_DNA.
DR   RefSeq; WP_012095503.1; NC_009674.1.
DR   AlphaFoldDB; A7GT08; -.
DR   SMR; A7GT08; -.
DR   STRING; 315749.Bcer98_3040; -.
DR   EnsemblBacteria; ABS23266; ABS23266; Bcer98_3040.
DR   GeneID; 56418585; -.
DR   KEGG; bcy:Bcer98_3040; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002300; 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_1000079215"
FT   REGION          581..611
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;  65781 MW;  0B9D5B81B88EB993 CRC64;
     MSKIIGIDLG TTNSCVAVME GGEPKVIPNP EGNRTTPSVV AFKNDERQVG EVAKRQAITN
     PNTIMSIKRH MGTDYKVEIE GKKYTPQEIS AIILQNLKAS AEAYLGEPVT KAVITVPAYF
     NDAERQATKD AGRIAGLEVE RIINEPTAAA LAYGLEKQDE EQKILVYDLG GGTFDVSILE
     LADGTFEVIS TAGDNRLGGD DFDQVIIDYL VAEFKKENNI DLSQDKMALQ RLKDAAEKAK
     KDLSGVTQTQ ISLPFISAGA AGPLHLELNL TRAKFEELSA NLVERTLEPT RRALKDAGLS
     ASDLDKVILV GGSTRIPAVQ EAIKRETGKE PYKGVNPDEV VALGAAVQGG VLTGDVEGVL
     LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPPAPRGIP QIEVTFDIDA NGIVNVRAKD LGTNKEQAIT IQSSSGLSDE
     EVERMVKEAE ANADADQKRK EEVELRNEAD QLVFQTDKVV KDLEGKVDAA EVAKATEAKD
     ALKAAIEKND LDEIRAKKDA LQEIVQQLTV KLYEQAQAAA GAQQAEGAQG NAGAKNDNVV
     DAEFEEVKED K