ID   DNAK_CALS8              Reviewed;         606 AA.
AC   A4XKA4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Csac_1752;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA   VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA   Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA   Kengen S.M.W., Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) 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; CP000679; ABP67339.1; -; Genomic_DNA.
DR   RefSeq; WP_011917273.1; NC_009437.1.
DR   AlphaFoldDB; A4XKA4; -.
DR   SMR; A4XKA4; -.
DR   STRING; 351627.Csac_1752; -.
DR   PRIDE; A4XKA4; -.
DR   EnsemblBacteria; ABP67339; ABP67339; Csac_1752.
DR   KEGG; csc:Csac_1752; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000256; 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..606
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059528"
FT   REGION          578..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   606 AA;  66452 MW;  4557819EB24DB0FD CRC64;
     MAHILGIDLG TTNSCMAVIE GGQPVVIPNA EGFRTTPSVV AFTKTGERLV GHAAKRQAIT
     NPERTIISIK RDMGTNRRIK IDDKEYSPEE ISAMILMKLK ADAEAYLGEK ITQAVITVPA
     YFTDSQRQAT KNAGRIAGLE VLRIINEPTA AALAYGLDKE GHQKIMVYDL GGGTFDVSIL
     EIGEGVIEVL ATSGNNRLGG DDFDQRIIDY IADEFMKEHG IDLRKDKVAL QRLKDAAERA
     KIELSSALQT TINLPFITAD ANGPKHIDMV LTRAKFEELI KDLVEKTREP VETALSDAKL
     TPEQIDKVIL VGGSTRIPYV QEFVKKLTGK EPFKGINPDE CVAIGAAIQA GVLGGQVKDI
     LLLDVTPLSL GIETLGGVFT KIIERNTTIP TRKSQIFTTA ADGQTQVEIH VLQGERPLAK
     DNKTLGRFIL DGIPPAPRGV PQIEVTFDID ANGIVHVSAK DLGTGREQKI TITSQTHLSE
     EEIQRAIKEA EMYAEQDRKR KELIETRNKA DSIIYQTEKL LRDLGDKMTA TEKEQIEAKL
     KALKDVMNGE DKERIERAID ELTKSFYDVS TRLYQQGYTQ AGPQGGTNPG GQGGTDGNVN
     TDYKVY