ID   DNAK_CLOB1              Reviewed;         623 AA.
AC   A7FXL5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=CLB_2923;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000726; ABS32890.1; -; Genomic_DNA.
DR   RefSeq; WP_003357980.1; NC_009697.1.
DR   AlphaFoldDB; A7FXL5; -.
DR   SMR; A7FXL5; -.
DR   GeneID; 5184256; -.
DR   KEGG; cba:CLB_2923; -.
DR   HOGENOM; CLU_005965_2_4_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; 2.
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_1000059539"
FT   REGION          580..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;  66832 MW;  9328C79FF262D23E CRC64;
     MAKIIGIDLG TTNSCVSVME GGEPVVIPNA EGSRTTPSVV SFQANGERLI GQVAKRQAIT
     NPEKTIISIK RYMGTDHKVN IDSTEYTPQQ 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 RKESIEIKNN ADQIVYQTEK TLTDLGDKVS AEDKAQIEEK
     VKAVKDVKDG EDLEAIKKAT EDLTQTFYGI SSKIYQQANP EGAQGAGFDP NNMGGANAGN
     ASAGNDKKDD NVVDADFKVE DDK