DNAK_THEYD
ID DNAK_THEYD Reviewed; 632 AA.
AC B5YH59;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=THEYE_A1758;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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; CP001147; ACI20675.1; -; Genomic_DNA.
DR RefSeq; WP_012545409.1; NC_011296.1.
DR RefSeq; YP_002249549.1; NC_011296.1.
DR AlphaFoldDB; B5YH59; -.
DR SMR; B5YH59; -.
DR STRING; 289376.THEYE_A1758; -.
DR PRIDE; B5YH59; -.
DR EnsemblBacteria; ACI20675; ACI20675; THEYE_A1758.
DR KEGG; tye:THEYE_A1758; -.
DR PATRIC; fig|289376.4.peg.1714; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_0; -.
DR InParanoid; B5YH59; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000718; 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; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..632
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119770"
FT REGION 599..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 632 AA; 69290 MW; DAE336984A3DA4F7 CRC64;
MGKAIGIDLG TTNSVVAVVV GGEPVVIPNQ EGQRTTPSVV AFTDKGERLV GQVAKRQAIT
NPENTIFSIK RLMGRKYNSQ EVQEAKKRLP YKIVEAPNGD AHVEIMGKRY SPPEISAMIL
QKLKQAAEDY LGEPVTEAVI TVPAYFDDSQ RQATKDAGRI AGLNVLRIIN EPTAAALAYG
LDKKKEEKIA VYDLGGGTFD ISILEIGEGV IEVKATNGDT YLGGDDFDIR VMDWLIEEFK
KQEGIDLRKD RMALQRLKEA AERAKIELSS AMETEINLPF ITADASGPKH LLMKLTRAKL
EQLVDDLIQK SLEPCKKALS DAGLSQSQID EVILVGGQTR TPKVQKVVQD FFGKEPHKGV
NPDEVVAVGA AIQAAILKGE VKEVLLLDVT PLSLGIETLG GVFTKIIERN TTIPTKKSQI
FTTAADNQTA VTIKVYQGER EMAADNKLLG VFELVGIPPA PRGIPQIEVT FDIDANGILH
VSAKDLATGK EQSIRITASS GLSEEEIKKM IREAEAHAEE DRRKKQIAEA RNEADNMIYT
VEKTLRDMGD RISEDERKRI EEAIEKCRRI KDTSNDVNEI KAAVEELAKA SHRVAEELYK
KAGASQQGAG STTQSKKEED VIEAEVEDKD NK