DNAK_THET2
ID DNAK_THET2 Reviewed; 615 AA.
AC Q72IK5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=TT_C1127;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81469.1; -; Genomic_DNA.
DR RefSeq; WP_011173541.1; NC_005835.1.
DR AlphaFoldDB; Q72IK5; -.
DR BMRB; Q72IK5; -.
DR SMR; Q72IK5; -.
DR STRING; 262724.TT_C1127; -.
DR PRIDE; Q72IK5; -.
DR EnsemblBacteria; AAS81469; AAS81469; TT_C1127.
DR KEGG; tth:TT_C1127; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_0; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000592; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..615
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226023"
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:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 615 AA; 66810 MW; 904DE75DC86E3E88 CRC64;
MAKAVGIDLG TTNSVIAVLE GGKPVVLENA EGERVTPSVV AFRDGETLVG RMAKRQAVLN
PEGTIFEIKR FIGRRFEEVQ EEAKRVPYKV VPGPDGGVRV EVKGKLYTPE EISAMILRKL
VEDASKKLGE KITKAVITVP AYFNNAQREA TANAGRIAGL EVLRIINEPT AAALAYGLDK
KGNETVLVFD LGGGTFDVTV 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
