ID   DNAK_CLOB6              Reviewed;         623 AA.
AC   C3L3G7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=CLJ_B3216;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
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; CP001083; ACQ54917.1; -; Genomic_DNA.
DR   RefSeq; WP_003359986.1; NC_012658.1.
DR   AlphaFoldDB; C3L3G7; -.
DR   SMR; C3L3G7; -.
DR   EnsemblBacteria; ACQ54917; ACQ54917; CLJ_B3216.
DR   KEGG; cbi:CLJ_B3216; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002333; 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..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205180"
FT   REGION          578..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..623
FT                   /note="Basic and acidic residues"
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   623 AA;  66842 MW;  06322AD7503DFC70 CRC64;
     MAKIIGIDLG TTNSCVSVME GGEPVVIPNA EGSRTTPSVV SFQANGERLI GQVAKRQAIT
     NPEKTIISIK RYMGTDHKVN IDNTEYTPQQ ISAMVLQKLK ADAEAYLGEK VTQAVITVPA
     YFNDSQRQAT KDAGKIAGLE VLRIINEPTA ASLAYGLDKM DTNEKILVYD LGGGTFDVSI
     LELGDGVFEV KATNGDTKLG GDDFDQKLID YIAETFKAEN GIDLRNDKMA IQRLKEAAEK
     AKIELSSATQ TNINLPFITA DATGPKHIDM NLTRAKFNEL THDLVQRTLE PIKKSLEGSG
     YAMSDIDKII MVGGSTRIPA VQDAVKDFTG KELSKGVNPD EVVAMGAAIQ AGVLTGEVKD
     VLLLDVTPLT LGIETFGGVS TTLIEKNTTI PTRKSQVFST AADGQTSVEI HVVQGERSMA
     ADNKTLGRFT LSGIAPAPRG IPQIEVTFDI DANGIVNVSA KDKGTGKEAN ITITASTNLT
     DDEIEKAVNE AKKFEAEDKK RKESIEVKNN ADQIVYQTEK TLTDLGDKVS AEDKAQIEEK
     VKVVKDVKDG EDLEAIKKAT EDLTQTFYGI SSKIYQQANP EGAPGAGFDP NNMGGANAGN
     ASAGNDKKDD NVVDADFKVE DDK