DNAK_THET8
ID DNAK_THET8 Reviewed; 615 AA.
AC Q56235; P77648; Q5SI83;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
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; OrderedLocusNames=TTHA1491;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9349721; DOI=10.1016/s0167-4781(97)00071-7;
RA Osipiuk J., Joachimiak A.;
RT "Cloning, sequencing, and expression of dnaK-operon proteins from the
RT thermophilic bacterium Thermus thermophilus.";
RL Biochim. Biophys. Acta 1353:253-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Seidel R.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9276481; DOI=10.1016/s0014-5793(97)00847-8;
RA Motohashi K., Yohda M., Odaka M., Yoshida M.;
RT "K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of
RT DnaK/DnaJ complex from Thermus thermophilus.";
RL FEBS Lett. 412:633-636(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10377389; DOI=10.1073/pnas.96.13.7184;
RA Motohashi K., Watanabe Y.H., Yohda M., Yoshida M.;
RT "Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB
RT chaperones.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7184-7189(1999).
RN [6]
RP REGULATION OF THE DNAK CHAPERONE SYSTEM.
RX PubMed=10092456; DOI=10.1006/jmbi.1999.2636;
RA Klostermeier D., Seidel R., Reinstein J.;
RT "The functional cycle and regulation of the Thermus thermophilus DnaK
RT chaperone system.";
RL J. Mol. Biol. 287:511-525(1999).
CC -!- FUNCTION: Cooperates with DnaJ, GrpE and ClpB to reactivate heat-
CC inactivated proteins. {ECO:0000269|PubMed:10377389}.
CC -!- SUBUNIT: Forms a heterononamer with DnaJ and DafA in the resting state.
CC Three copies of each protein are present in the complex.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In the resting state, the DnaK-DnaJ-DafA complex cannot
CC bind substrate. As the substrate becomes sufficiently high, DafA is
CC displaced and an active DnaK-substrate-DnaJ complex is formed.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L57504; AAB04676.1; -; Genomic_DNA.
DR EMBL; Y07826; CAA69159.1; -; Genomic_DNA.
DR EMBL; D84222; BAA12280.1; -; Genomic_DNA.
DR EMBL; AB012390; BAA81741.1; -; Genomic_DNA.
DR EMBL; AB032368; BAA96089.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71314.1; -; Genomic_DNA.
DR RefSeq; WP_011228715.1; NC_006461.1.
DR RefSeq; YP_144757.1; NC_006461.1.
DR PDB; 6PRP; NMR; -; A=604-615.
DR PDBsum; 6PRP; -.
DR AlphaFoldDB; Q56235; -.
DR BMRB; Q56235; -.
DR SMR; Q56235; -.
DR STRING; 300852.55772873; -.
DR EnsemblBacteria; BAD71314; BAD71314; BAD71314.
DR GeneID; 3167961; -.
DR KEGG; ttj:TTHA1491; -.
DR PATRIC; fig|300852.9.peg.1466; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_0; -.
DR OMA; ISIKRHM; -.
DR PhylomeDB; Q56235; -.
DR Proteomes; UP000000532; 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; 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; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..615
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078574"
FT REGION 592..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 360..363
FT /note="NPDE -> EPRTK (in Ref. 1; AAB04676)"
FT /evidence="ECO:0000305"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:6PRP"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:6PRP"
SQ SEQUENCE 615 AA; 66824 MW; EA7CCA0F78362C94 CRC64;
MAKAVGIDLG TTNSVIAVLE GGKPVVLENA EGERVTPSVV AFRDGETLVG RMAKRQAVLN
PEGTIFEIKR FIGRRFEEVQ EEAKRVPYKV VPGPDGGVRV EVKGKLYTPE EISAMILRKL
VEDASKKLGE KITKAVITVP AYFNNAQREA TANAGRIAGL EVLRIINEPT AAALAYGLDK
KGNETVLVFD LGGGTFDVTI LEIGEGVFEV KATSGDTHLG GSDMDHAIVN WLAEEFKKEH
GVDLKADRQA LQRLIEAAEK AKIELSSTLE TTISLPFIAL DPASKTPLHL EKKLTRAKFE
ELIQPLLKRL RGPVEQALKD AGLTPAQIDE VILVGGATRV PAVQQVVREL LGKEPNRSVN
PDEVVAMGAA IQAGVLMGEV RDVVLLDVTP LSLGVETKGG VMTVLIPRNT TIPTRKCEIF
TTAEHNQTAV EIHVLQGERP MAQDNKSLGR FRLEGIPPMP AGVPQIEVCF DIDANGILHV
TAKERSTGRE ASITIQNTTT LSEEEIQRII EEAKRHAEED RRRREHAELK NALDSARVQA
ERVLQERQGA PEARARLEAA IGKAKELVER DAPDPELKAA TEELLKAVEE YEKGAQAASG
KGPDDVIDAD YKPAD
