ID   DNAK_THEMA              Reviewed;         596 AA.
AC   Q9WYK6; Q9ZFD2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; Synonyms=hsp70; OrderedLocusNames=TM_0373;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Michelini E.T., Flynn G.C.;
RT   "The unique chaperone operon of Thermotoga maritima: cloning and initial
RT   characterization of a functional Hsp70 and sHsp.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF106330; AAC79725.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35460.1; -; Genomic_DNA.
DR   PIR; C72385; C72385.
DR   PIR; T46657; T46657.
DR   RefSeq; NP_228184.1; NC_000853.1.
DR   RefSeq; WP_004083187.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WYK6; -.
DR   SMR; Q9WYK6; -.
DR   STRING; 243274.THEMA_02850; -.
DR   PRIDE; Q9WYK6; -.
DR   EnsemblBacteria; AAD35460; AAD35460; TM_0373.
DR   KEGG; tma:TM0373; -.
DR   eggNOG; COG0443; Bacteria.
DR   InParanoid; Q9WYK6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008183; 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; 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..596
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078572"
FT   MOD_RES         180
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1..9
FT                   /note="MAEKKEFVV -> MSKII (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="A -> P (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="Y -> F (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138..140
FT                   /note="AGI -> S (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="D -> PLP (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="I -> T (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        434
FT                   /note="I -> M (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534
FT                   /note="E -> D (in Ref. 1; AAC79725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   596 AA;  66052 MW;  7478381447DC420E CRC64;
     MAEKKEFVVG IDLGTTNSVI AWMKPDGTVE VIPNAEGSRV TPSVVAFTKS GEILVGEPAK
     RQMILNPERT IKSIKRKMGT DYKVRIDDKE YTPQEISAFI LKKLKNDAEA YLGGEIKKAV
     ITCPAYFNDA QRQATKEAGI IAGLEVLRII NEPTAAALAY GLDKAGKEEK VLVYDLGGGT
     FDVSILEIGE GVIEVIATAG NNHLGGDDFD QRLIDWMAEE FKKQHGIDLR EDRQALQRLR
     DAAEKAKIEL STKMETDVSL PFIAVSPSGQ PLHLEMRITR SLFESLTRDL VEMTRGPIEQ
     ALNDAKLSPQ DIDEIILVGG MTRVPMVQRF IKEFFGKEPN KSVNPDEAVA IGAAIQAAIL
     AGTEGAKGRD IVLVDVTPLT LGIEVKGGLF EPIIPRNTKI PVRKSKIFTT VEDGQTEVEI
     RVYQGERPIA RENIFLGSFK LVGIPPAPRG VPQIEVTFDI DSDGIVHVSA KDLGSGKEQS
     MVVTGRHKLS EDEIKRMIED AKRYEEQDKR LKEEIELKNR ADDLAYSVEK TLKEHGDKIP
     ADLKSRLEDM IRELRDAINR NDIPKVKMLF DDLQKESMKI GEYLYKSATG GETSNQ