ID   DNAK_THEPX              Reviewed;         612 AA.
AC   B0K3Y0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-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};
GN   OrderedLocusNames=Teth514_2079;
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter;
OC   unclassified Thermoanaerobacter.
OX   NCBI_TaxID=399726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) 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; CP000923; ABY93351.1; -; Genomic_DNA.
DR   RefSeq; WP_009052596.1; NC_010320.1.
DR   AlphaFoldDB; B0K3Y0; -.
DR   SMR; B0K3Y0; -.
DR   PRIDE; B0K3Y0; -.
DR   EnsemblBacteria; ABY93351; ABY93351; Teth514_2079.
DR   KEGG; tex:Teth514_2079; -.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002155; 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..612
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119768"
FT   REGION          578..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..601
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   612 AA;  66535 MW;  18E6E6FC55E7D502 CRC64;
     MGKVIGIDLG TTFSCVAVME GGQPVVIPNA EGARTTPSVV AFTKEGERLV GQVAKRQAIV
     NPDRTIMSIK RHMGSDYKVK IDDKEYTPQE ISAMILQKLK ADAEAYLGEK VTQAVITVPA
     YFNDSQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKE GNQKIMVYDL GGGTFDVSIL
     EIGEGVFEVL ATSGNNHLGG DDFDQRIIDW LADNFKKEHG IDLRNDRMAL QRLKDAAERA
     KIELSSATVT NINLPFITAD ATGPKHIDVN LTRAKFEELI SDLVESTVGP VNQALNDAGL
     KPSDIDKVLL IGGSTRVPLV QETVKKIMGK EPHKGINPDE AVAIGAAIQA AVLSGEVKDI
     LLLDVTPLSL GIETLGGVFT KIIERNTTIP TRKSQIFTTA ADNQTSVEIH VLQGERPMAK
     DNKTLGRFIL SGIPPAPRGV PQIEVTFDID ANGIVHVSAK DLGTGKSQDI TITSTTNLSE
     EEIQRMINEA KQYEEQDRKK KEEIEIRNKA DSLIYQAEKT MKDLGDKMTQ AEKDEINKEI
     ENVRKALEGS DIEAIKSASE KLSQAFYKVS TRIYQQAGGQ TGGATNTDSA GQGTTQDNVY
     EANYKVEDDD NK