ID   DNAK_CLOBA              Reviewed;         616 AA.
AC   B2V2I5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CLH_0858;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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; CP001078; ACD51747.1; -; Genomic_DNA.
DR   RefSeq; WP_003369488.1; NC_010723.1.
DR   AlphaFoldDB; B2V2I5; -.
DR   SMR; B2V2I5; -.
DR   PRIDE; B2V2I5; -.
DR   KEGG; cbt:CLH_0858; -.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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..616
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119688"
FT   REGION          579..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   616 AA;  65821 MW;  131E86BA17D89682 CRC64;
     MGKIIGIDLG TTNSCVAVME GGEPVVITNS EGARTTPSVV SFQADGERLV GQVAKRQSIT
     NPDKTIISIK RHMGTSYKVD IDGKNYSPQE ISAMVLQKIK ADAESYLGES VTQAVITVPA
     YFNDSERQAT KDAGKIAGLE VLRIINEPTA AALAYGLDKM DSNHKILVYD LGGGTFDVSI
     LELGDGVFEV LSTNGDTKLG GDDFDQKVMD YIAETFKAEN GIDLRQDKMA LQRLKEAAEK
     AKIELSSSMQ TNINLPFITA DATGPKHIDL NLTRAKFNEI THDLVQRSIE PMKKALSDAA
     ISIDEIEKII LVGGSTRIPA VVEAVKNFTG KDPSKGVNPD ECVAVGAAVQ AGVLTGEVKD
     VLLLDVTPLT LGIETAGGIA TPLIERNTTI PTKKSQIFST AADSQTSVEI NVVQGERQMA
     MDNKSLGRFT LSGIAPAPRG IPQIEVTFDI DANGIVKVSA LDKGTGKEAN ITITASTNLN
     DEEIDKAVKE AEKFAEEDKK RKEKVETLNN ADQLIYQTEK ALTELGDKVS AEDKAKVTEK
     LEALKAIKDG EDLEAIKKAT EELTQEFYAV SSKVYAAAGG DPSQAGGFDP NAAGGAQQAP
     HDDNVVDADF KVDDDK