DNAK_THEP1
ID DNAK_THEP1 Reviewed; 596 AA.
AC A5IK42;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Tpet_0544;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000702; ABQ46565.1; -; Genomic_DNA.
DR RefSeq; WP_004083187.1; NC_009486.1.
DR AlphaFoldDB; A5IK42; -.
DR SMR; A5IK42; -.
DR STRING; 390874.Tpet_0544; -.
DR EnsemblBacteria; ABQ46565; ABQ46565; Tpet_0544.
DR KEGG; tpt:Tpet_0544; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_0; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000006558; 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 Stress response.
FT CHAIN 1..596
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059692"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
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
