DNAK_THEVO
ID DNAK_THEVO Reviewed; 613 AA.
AC Q97BG8;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=TV0487;
GN ORFNames=TVG0471466;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-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; BA000011; BAB59629.1; -; Genomic_DNA.
DR RefSeq; WP_048054084.1; NC_002689.2.
DR AlphaFoldDB; Q97BG8; -.
DR SMR; Q97BG8; -.
DR STRING; 273116.14324702; -.
DR EnsemblBacteria; BAB59629; BAB59629; BAB59629.
DR GeneID; 1441004; -.
DR KEGG; tvo:TVG0471466; -.
DR eggNOG; arCOG03060; Archaea.
DR HOGENOM; CLU_005965_2_4_2; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 10764at2157; -.
DR PhylomeDB; Q97BG8; -.
DR Proteomes; UP000001017; 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; Stress response.
FT CHAIN 1..613
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078603"
FT REGION 579..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 66473 MW; 9A3F6F0586F78936 CRC64;
MSKIIGIDLG TSNSAAAVVI SGKPTVIPSS EGVSIGGKAF PSYVAFTKDG QMLVGEPARR
QALLNPEGTI FAAKRKMGTD YKFKVFDKEF TPQQISAFIL QKIKKDAEAF LGEPVNEAVI
TVPAYFNDNQ RQATKDAGTI AGFDVKRIIN EPTAAALAYG VDKSGKSEKI LVFDLGGGTL
DVTIIEISKR PNVQVLSTSG DTQLGGTDMD EAIVNYIADD FQKKEGIDLR KDRGAYIRLR
DAAEKAKIEL STTLSSDIDL PYITVTSSGP KHIKMTLTRA KLEELISPIV ERVKAPIDKA
LEGAKLKKTD ITKLLFVGGP TRIPYVRKYV EDYLGIKAEG GVDPMEAVAI GAAIQGAVLK
GEIKDIVLLD VTPLTLSVET LGGIATPIIP ANTTIPVRKS QVFTTAEDMQ TTVTIHVVQG
ERPLAKDNVS LGMFNLTGIA PAPRGIPQIE VTFDIDSNGI LNVTAVDKAT GKKQGITITA
STKLSKDEIE RMKKEAEQYA EQDRKMKEQI ETLNNAESLA YSVEKTLNEA GDKVDKETKD
RILSEVKDLR KAIEEKNMDN VKTLMEKISK DIQEVGTKMY QSASSTTQTG SGNQNSSKQE
NDKTVDAEYK EKS