ID   DNAK_THEFY              Reviewed;         613 AA.
AC   Q47TI0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Tfu_0196;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54234.1; -; Genomic_DNA.
DR   RefSeq; WP_011290643.1; NC_007333.1.
DR   AlphaFoldDB; Q47TI0; -.
DR   SMR; Q47TI0; -.
DR   STRING; 269800.Tfu_0196; -.
DR   PRIDE; Q47TI0; -.
DR   EnsemblBacteria; AAZ54234; AAZ54234; Tfu_0196.
DR   KEGG; tfu:Tfu_0196; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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; 2.
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..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226022"
FT   REGION          495..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..535
FT                   /note="Basic and acidic 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   613 AA;  66042 MW;  F93267862FBE26E2 CRC64;
     MARAVGIDLG TTNSVVAVLE GGEPTVIANA EGARTTPSVV AFAKNGEVLV GEIAKRQAVT
     NVERTIRSVK RHMGTDWKTH IDGKDFTPQQ ISAFVLQKLK RDAEAYLGEE VTDAVITVPA
     YFSDAERQAT KDAGKIAGLN VLRIINEPTS AALAYHLEKE GEATILVFDL GGGTFDVSLL
     DVGDGVVEVK ATHGDNHLGG DDWDQAVVDW LVERFKSSNG IDLSKDKMAM QRLREAAEKA
     KIELSSSTET SINLPYITAS AEGPLHLDEK LTRAEFQRLT SHLLERTKGP FFQVIKDAGI
     SVDQIDHVVL VGGSTRMPAV VDLVRELTGG KEPNKGVNPD EVVAVGAALQ AGVLKGDVKD
     VLLLDVTPLS LGIETKGGVF TKLIERNTAI PTKRSEIFTT AEDNQPSVQI QVYQGEREIA
     KYNKKLGVFD LTGIPPAPRG VPQIEVTFDI DANGIVNVTA KDLGTGKEQS VTITGGSALP
     KEDIERMIRE AEEYAEQDRK RREEAETRNN AESLVYQTEK VISENEDKIP EDVKNETKEA
     LDGLKKALEG SDIEAIRSAS EKVALASQKI GSAIYSQSQQ ASGAAAGGQQ NAEDAEVVDA
     EIVDEEPKRE GNS