ID   DNAK_THEAB              Reviewed;         598 AA.
AC   B7ID00;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=THA_1433;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ75877.1; -; Genomic_DNA.
DR   RefSeq; WP_004101858.1; NC_011653.1.
DR   AlphaFoldDB; B7ID00; -.
DR   SMR; B7ID00; -.
DR   STRING; 484019.THA_1433; -.
DR   PRIDE; B7ID00; -.
DR   EnsemblBacteria; ACJ75877; ACJ75877; THA_1433.
DR   KEGG; taf:THA_1433; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002453; 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..598
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119766"
FT   MOD_RES         180
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   598 AA;  66259 MW;  2AC380DCC81A3ED3 CRC64;
     MANKKEYVVG IDLGTTNSVI AWMKPDSSVE VIPNAEGART TPSIVAFSKT GEILVGEPAK
     RQLILNSERT IKSIKRKMGT DYKVKIDDKD YTPQEISAFI LKKLKRDAEE YLGGEVKKAV
     ITCPAYFNDA QRQATKEAGI IAGFEVLRII NEPTAAALAY GLDKKGKEEK VLVYDLGGGT
     FDVSILEIGD GVIQVVATSG NNHLGGDDFD QRIIDWLAEE FKKQHGVDLR EDKQALQRLR
     DAAEKAKIEL SSKLETDISL PYITATAEGP LHLEMRLTRS MFESLTRDLV EMTRKPVEQA
     LSDAKLKPED IDEIILVGGM TRVPMVQKFI KEIFGKDPNR GVNPDEAVAV GAAIQAAILA
     GEEGAQGKDI VLVDVTPLTL GIEVKGGLFE PIIPRNSTIP IKKSKVFTTA EDGQTEVEVR
     VYQGERPIAA DNILLGSFRL VGIPPAPRGV PQIEVTFDID SDGIVHVSAK DLGTGKEQSM
     VVSGRHQLSE DDINKIIEDA KKFEEQDKRR KEEVELKNKA DDLAYYIEKS LKEYGDKIPA
     DEKDKLENLV KDLRDAINKN DIPRIKMLFD ELDREKTKIG EYIYKQNQQG GNQQAENQ