ID   DNAK_CLONN              Reviewed;         617 AA.
AC   A0Q1R4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=NT01CX_0057;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK62104.1; -; Genomic_DNA.
DR   RefSeq; WP_011722558.1; NC_008593.1.
DR   AlphaFoldDB; A0Q1R4; -.
DR   SMR; A0Q1R4; -.
DR   STRING; 386415.NT01CX_0057; -.
DR   PRIDE; A0Q1R4; -.
DR   EnsemblBacteria; ABK62104; ABK62104; NT01CX_0057.
DR   KEGG; cno:NT01CX_0057; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008220; 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   Reference proteome; Stress response.
FT   CHAIN           1..617
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059543"
FT   REGION          578..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..617
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   617 AA;  66306 MW;  65399ED418A7303B CRC64;
     MGKIIGIDLG TTNSCVSVME GGNPVVIPNA EGSRTTPSVV AFKEDGERLV GQVAKRQAIT
     NPDKTIISIK RHMGTDYRVN VDGKDYSPEE ISAMILQKLK ADAEAYLGET VTEAVITVPA
     YFNDSERQAT KNAGKIAGLD VKRIINEPTA ASLAYGLDKM DKSHKIFVYD LGGGTFDVSI
     LELGDGVFEV KATNGNTKLG GDDFDQKIMD YIAETFKAEN GIDLRNDKMA LQRLKEAAEK
     AKIELSSSTK TNINLPFITA DATGPKHIDM DLTRAKFEEL SADLVQATIE PMKKALADAE
     LTINDIDKVV LVGGSTRIPA VQEAVQKFTG KEPSKGVNPD EVVAMGAAVQ AGVLTGEVKD
     ILLLDVTPLT LGIETMGGVA TPLIERNTTI PTRKSQIFST AADNQTSVDI HIVQGERKMA
     GDNKTLGRFQ LSGIAPAPRG IPQIEVSFDI DANGILNVSA KDKGTGKEAN ITITASTNLS
     DDEIDKAVKE AEKFAAEDEK RKESVEVKNN ADSALYQTEK ALKDLGDKVE EADKKNVEEK
     LEALRQVKDG EDLEAIKKAT TELTEEFYKV SSKLYQQAGA EAQQGAQGTQ GADMGGNAQG
     KDDDNVVDAD FKVEDDK