ID   DNAK_CALS4              Reviewed;         606 AA.
AC   Q8RB68;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=TTE0955;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM24211.1; -; Genomic_DNA.
DR   RefSeq; WP_011025330.1; NC_003869.1.
DR   AlphaFoldDB; Q8RB68; -.
DR   SMR; Q8RB68; -.
DR   STRING; 273068.TTE0955; -.
DR   PRIDE; Q8RB68; -.
DR   EnsemblBacteria; AAM24211; AAM24211; TTE0955.
DR   KEGG; tte:TTE0955; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000555; 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..606
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078575"
FT   REGION          576..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..594
FT                   /note="Polar residues"
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;  66029 MW;  0BEF79EA16892809 CRC64;
     MGKVIGIDLG TTFSCVAVME GGQPVVIPNS EGTRTTPSVV AFTKEGERLV GHPARRQAII
     NPERTIMSIK RHMGTDYKVK IDDKEYTPQE ISAMILQKLK ADAEAYLGEK VTQAVITVPA
     YFNDSQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKE GNQKVMVYDL GGGTFDVSIL
     EIGDGVFEVL ATSGNNHLGG DDFDQRIIDW LADNFQKEHG IDLRKDRMAL QRLKEAAERA
     KIELSSAMVT NINLPFITAD ASGPKHIDVN LTRAKFEELI SDLVESTVGP VKQALSDAGL
     KPEDIDKVLL VGGSTRIPLV QETVKKIMGK EPHKGINPDE AVAIGAAIQA AVLAGEIKDI
     LLLDVTPLSL GIETLGGVFT KIIERNTTIP VRKSQIFTTA ADNQTSVEIH VLQGERPLAK
     DNKSLGRFIL SGIPPAPRGV PQIEVTFDID ANGIVHVSAK DLATGKSQQI TITGSTNLSE
     EEIQRMINEA KQYEEQDRKK REEIEIRNRA DSLIYQAEKT MKDLGDKMTQ AEKDEINKEI
     ENVRKALEGT DVEAIKAASE KLSEAFYKVS TRLYQQAAGS ANPGGSQGTS QGNVYEADYK
     VEDDNK