DNAK_DESOH
ID DNAK_DESOH Reviewed; 642 AA.
AC A8ZRW3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Dole_0070;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-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; CP000859; ABW65880.1; -; Genomic_DNA.
DR RefSeq; WP_012173499.1; NC_009943.1.
DR AlphaFoldDB; A8ZRW3; -.
DR SMR; A8ZRW3; -.
DR STRING; 96561.Dole_0070; -.
DR PRIDE; A8ZRW3; -.
DR EnsemblBacteria; ABW65880; ABW65880; Dole_0070.
DR KEGG; dol:Dole_0070; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008561; 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; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119699"
FT REGION 594..642
FT /note="Disordered"
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 642 AA; 68730 MW; D978DBA95B6E3367 CRC64;
MAKTIGIDLG TTNSCVAVME GGEAKVITNP EGGRTTPSIV AINEDGERLV GQVAKRQAIT
NPENTVFGVK RLIGRKFDSA EVQHDIKVLP YKIEKAGNGD LRINLRDKQY SPAEISSFIL
ADIKHTAEEY LGEKVTDAVI TVPAYFSDSQ RQATKDAGKI AGLNVLRIIN EPTAASLAYG
LDKKKDEKIA VFDLGGGTFD ISVLEIGDGV FEVKSTNGDT HLGGEDFDLR VVDYLASEFK
KDQGIDLRQD KMALQRLKEA AEKAKMELSS SPQTDINLPF ITADANGPKH LNIKLSRAKL
EELVEDLLDK MAKPCETALK DSGFSASQID EVILVGGMTR MPAVQDRVKK IFGKAPNKSV
NPDEVVAIGA AIQAGVLQGD VNDVLLLDVT PLSLGIETLG GVMTKLIEKN TTIPTKKSQV
FSTAADNQPA VSIHVLQGER EMAANNKTLG RFDLADIPAA PRGVPQIEVT FDIDANGIVA
VSAKDLGTGK EQSIKITASS GLSKEEIDKL VKDAEAHAEE DKNKRELVEA QNTADALIYQ
TEKSIKELGE DKLDNATKAE IQAKIEELKK AKETTDTDQI KKLSDELTQA SHKLAEAMYQ
KASQEGQQAS GGDAGASADG GTSSAAGGDD DVIDADYEEA GK