ID   DNAK_DICTD              Reviewed;         607 AA.
AC   B8DYH6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Dtur_0017;
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=515635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310;
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK41358.1; -; Genomic_DNA.
DR   RefSeq; WP_012582444.1; NC_011661.1.
DR   RefSeq; YP_002351972.1; NC_011661.1.
DR   AlphaFoldDB; B8DYH6; -.
DR   SMR; B8DYH6; -.
DR   STRING; 515635.Dtur_0017; -.
DR   EnsemblBacteria; ACK41358; ACK41358; Dtur_0017.
DR   KEGG; dtu:Dtur_0017; -.
DR   PATRIC; fig|515635.4.peg.17; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_0; -.
DR   InParanoid; B8DYH6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000007719; 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..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119702"
FT   REGION          577..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..597
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   607 AA;  66977 MW;  F3F789F4A5F849F3 CRC64;
     MAKIVGIDLG TTNSLIAYLE GGRPVIIPNA EGSRLTPSIV AFTKDGQLLV GEPAKRQAIV
     NAERTIRSIK RHMGTNYKVK IDDKEYTPQE ISAMILRKLK RDAEAYLGEK IEKAVITVPA
     YFSDAQRQAT KDAGAIAGLE VVRIINEPTA AALAYGLDKE GHQKILVFDL GGGTFDVSIL
     EIGEGVFEVI ATAGNNRLGG DDFDERIVNW LIENFMEEHG INLREDKTAL QRLYEAAEKA
     KIELSSKLQT EINLPFIAMK GNTPLHLSYT LTRAKFEELT YDLVEKTKEP TERALKDAGL
     SPSQIDKIIL VGGATRMPCI QEWIKKHFGK EPQRNVNPDE AVALGAAIQA GVIGGEIRDI
     VLVDVTPLSL GIETLGGVFT KIIERNTPIP VSKSQIFTTA ADYQTSVEIH VLQGERALAK
     DNISLGRFIL DGIPPAPRGV PQIEVTFDID VNGIVHVSAK DKATGREQRI TISNAIRLSE
     AEIKRMTEEA KRFEEEDRKR REEIETKNQA EHLIYTARKT LKDYGDKVSK DIVQKVEDKI
     KNLEELIKPE RINVEQVRKG MEELTQTLGE IGQFMYQSAG STAGNPGQGQ STENPGGKTI
     DGDYKVN