ID   DNAK_THEP3              Reviewed;         612 AA.
AC   B0KA81;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Teth39_1393;
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS   thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / DSM 2355 / 39E;
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., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA   Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
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; CP000924; ABY95044.1; -; Genomic_DNA.
DR   RefSeq; WP_003868077.1; NC_010321.1.
DR   AlphaFoldDB; B0KA81; -.
DR   SMR; B0KA81; -.
DR   STRING; 340099.Teth39_1393; -.
DR   EnsemblBacteria; ABY95044; ABY95044; Teth39_1393.
DR   KEGG; tpd:Teth39_1393; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002156; 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..612
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119767"
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;  66515 MW;  7F7A89CE0AD3171D CRC64;
     MGKVIGIDLG TTFSCVAVME GGQPVVIPNA EGARTTPSVV AFTKEGERLV GQVAKRQAIV
     NPDRTIMSIK RHMGTDYKVK IDDKEYTPQE ISAMILQKLK ADAEAYLGEK VTQAVITVPA
     YFNDSQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKE GNQKIMVYDL GGGTFDVSIL
     EIGDGVFEVL ATSGNNHLGG DDFDQRIIDW LADNFKKEYG IDLRNDRMAL QRLKDAAEKA
     KIELSSATVT NINLPFITAD ATGPKHIDVN LTRAKFEELI SDLVESTVGP VNQALSDAGL
     KPSDIDKVIL IGGSTRVPLV QETVKRIMGK EPHKGINPDE AVAIGAAIQA AVLAGEVKDI
     LLLDVTPLSL GIETLGGVFT KIIERNTTIP TRKSQIFTTA ADNQTSVEIH VLQGERPMAK
     DNKTLGRFIL SGIPPAPRGV PQIEVTFDID ANGIVHVSAK DLGTGKSQDI TITSTTNLSE
     EEIQRMINEA KQYEEQDRKK KEEIEIRNKA DSLIYQAEKT MKDLGDKMTQ AEKDEINREI
     ENVRKALEGS DIEAIKNASE KLSQAFYKVS TRIYQQAGGQ TGGATNTGSA GQGTTQDNVY
     EANYKVEDDD NK