ID   DNAK_THEAC              Reviewed;         613 AA.
AC   P50023;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 116.
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=Ta1087;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-594.
RX   PubMed=7704574; DOI=10.1016/s0960-9822(00)00249-9;
RA   Gupta R.S., Singh B.;
RT   "Phylogenetic analysis of 70 kD heat shock protein sequences suggests a
RT   chimeric origin for the eukaryotic cell nucleus.";
RL   Curr. Biol. 4:1104-1114(1994).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AL445066; CAC12215.1; -; Genomic_DNA.
DR   EMBL; L35529; AAC41460.1; -; Genomic_DNA.
DR   RefSeq; WP_010901497.1; NC_002578.1.
DR   AlphaFoldDB; P50023; -.
DR   SMR; P50023; -.
DR   STRING; 273075.Ta1087; -.
DR   EnsemblBacteria; CAC12215; CAC12215; CAC12215.
DR   GeneID; 1456598; -.
DR   KEGG; tac:Ta1087; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_3_2; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 10764at2157; -.
DR   Proteomes; UP000001024; 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; 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; Reference proteome.
FT   CHAIN           1..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078602"
FT   REGION          578..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        190
FT                   /note="G -> A (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="I -> Y (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="A -> SP (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="L -> V (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454..455
FT                   /note="ID -> MH (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525..528
FT                   /note="TLND -> SLKH (in Ref. 2; AAC41460)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   613 AA;  66351 MW;  ED476E83B0FD8BA4 CRC64;
     MSKIIGIDLG TSNSAAAVVI SGKPTVIPSS EGVSIGGKAF PSYVAFTKDG QMLVGEPARR
     QALLNPEGTI FAAKRKMGTD YKFKVFDKEF TPQQISAFIL QKIKKDAEAF LGEPVNEAVI
     TVPAYFNDNQ RQATKDAGTI AGFDVKRIIN EPTAAALAYG VDKSGKSEKI LVFDLGGGTL
     DVTIMDFGDG VFQVLSTSGD TRLGGTDMDE AIVNYIADDF QKKEGIDLRK DRSAYIRLRD
     AAEKAKIELS TTLSTDIDLP YITVTNSGPK HIKMTLTRAK LEELISPIVE RVKGPIDKAL
     EGAKLKKTEI TKLLFVGGPT RIPYVRKYVE DYLGIKAEGG VDPMEAVAIG AAIQGAVLKG
     EIKDIVLLDV TPLTLSVETL GGIATPIIPA NTTIPVRKSQ IFTTAEDMQT TVTIHVVQGE
     RPLAKDNVSL GMFNLTGIAP APRGVPQIEV TFDIDSNGIL NVTAVDKATG KKQGITITAS
     TKLSKEEIER MKKEAEQYAE QDRKAKEQIE LLNNAESLAY SVEKTLNDAG DKVDKETKER
     LTNEVKDLRK AIEEKNTENV KTLMDKLSKD IQEVGAKMYQ QASANTQQSA QSNSQNSGSS
     DGKTVDAEYK EKS