ID   DNAK_ENDTX              Reviewed;         621 AA.
AC   B1H009;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, 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=TGRD_358;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG13841.1; -; Genomic_DNA.
DR   RefSeq; WP_015423368.1; NC_020419.1.
DR   RefSeq; YP_001956302.1; NC_020419.1.
DR   AlphaFoldDB; B1H009; -.
DR   SMR; B1H009; -.
DR   STRING; 471821.TGRD_358; -.
DR   PRIDE; B1H009; -.
DR   EnsemblBacteria; BAG13841; BAG13841; TGRD_358.
DR   KEGG; rsd:TGRD_358; -.
DR   PATRIC; fig|471821.5.peg.586; -.
DR   HOGENOM; CLU_005965_2_4_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001691; 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..621
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119772"
FT   REGION          583..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         179
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   621 AA;  66762 MW;  DE59C6D1FF279A48 CRC64;
     MAKIIGIDLG TSNSAAAVME GGKTTLIPSA EGTTLGGKAF PSYVAFTKDG QLLVGEPARR
     QAVTNPEGTI NAFKRKMGTN YKYKVNGKEF TPQQLSAFIL QKIKKDSEAY LGETITKAVI
     TVPAYFNDDQ RQATKDAGAI AGLEVVRLVN EPTAASLAYG IDKVGKEQKI LVFDLGGGTL
     DVTIMEMGAE GTFEVLSTSG DTQLGGTDMD NALIDYIAED FKKTNGIDLR NDKMAVQRLK
     EAAEKAKIEL SNVLETDINL PFITADASGP KHLAMKFTRA TLENLVRHIV ERCKASIDQA
     VKDAKLTAET VTKIILVGGP TRMPIVQKFA EDHVGKKAER GIDPMECVCF GAAVQAAVLT
     GDVKDILLLD VTPLTLGLET MGGVRTSLID RNTTVPAKRS QVFSTAADNQ PSVEINVLQG
     ERAMAKDNLS LGRFMLDGIP PAPRGVPQIE VTFDIDANGI LHVSAKDKGT GKEQSIKISS
     STKLSKDDID KYVKEAEQYA SEDVKRKEEI EVRNEADNLI YSVEKSLKDH GDKVSADERL
     IIEQSLTAAK DALKGSDVAT IKSAKEALTT ASHKLAEVVY KASQVQDTQG AAQGQSQGNP
     QQTADNRGKV VDAEIVDENK E