DNAK_THENN
ID DNAK_THENN Reviewed; 596 AA.
AC B9KBT4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=CTN_0304;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-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}.
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; CP000916; ACM22480.1; -; Genomic_DNA.
DR RefSeq; WP_015918809.1; NC_011978.1.
DR AlphaFoldDB; B9KBT4; -.
DR SMR; B9KBT4; -.
DR STRING; 309803.CTN_0304; -.
DR PRIDE; B9KBT4; -.
DR EnsemblBacteria; ACM22480; ACM22480; CTN_0304.
DR KEGG; tna:CTN_0304; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_0; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000445; 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_1000133168"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 596 AA; 66048 MW; EB7593A47E298936 CRC64;
MAEKKEFVVG IDLGTTNSVI AWMKPDGTVE VIPNAEGSRI TPSVVAFTKS GEILVGEPAK
RQMILNPERT IKSIKRKMGT DYKVRIDDKE YTPQEISAFI LKKLKKDAEA YLGGEIKKAV
ITCPAYFNDA QRQATKEAGI IAGLEVLRII NEPTAAALAY GLDKAGKEQK VLVYDLGGGT
FDVSILEIGD 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 EEDIKRMIED AKRYEEQDKR LKEEIELKNR ADDLAYSVEK TLREHGDKIP
ADLKSKLENM IKELRDAINR NDIPRVKMLF DDLQKESMKI GEYLYKSATG GEATNQ
