ID   DNAK_CUPPJ              Reviewed;         647 AA.
AC   Q46XI7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Reut_A2785;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ62146.1; -; Genomic_DNA.
DR   RefSeq; WP_011298931.1; NC_007347.1.
DR   AlphaFoldDB; Q46XI7; -.
DR   SMR; Q46XI7; -.
DR   STRING; 264198.Reut_A2785; -.
DR   EnsemblBacteria; AAZ62146; AAZ62146; Reut_A2785.
DR   KEGG; reu:Reut_A2785; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226001"
FT   REGION          611..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   647 AA;  69804 MW;  3BA60B748E312113 CRC64;
     MGKIIGIDLG TTNSCVSILE GNTPKVIENS EGTRTTPSII AYMEDGEILV GAPAKRQAVT
     NPRNTLYAVK RLIGRKFEEK EVQKDIGLMP YSIVKADNGD AWVGVRDQKL APPQVSAEVL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     MDKNEKGDRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IIGEFKKDQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
     ITRAKLEALV EDLITRTIEP CRTAIKDAGV KVSEIDDVIL VGGMTRMPKV QEQVKEFFGK
     EARKDVNPDE AVAVGAAIQG SVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
     TKHAQVFSTA DDNQPAVTIK VYQGEREMAT GNKLLGEFNL EGIPPSPRGT PQIEVSFDID
     ANGILHVGAK DKATGKENRI TIKANSGLSE DEIQRMVKDA EANAEEDKKA RELADARNQA
     DALVHSTKKA VTEYGDKLEA GEKEKIEAAI KELEDAARGG DKAEIDAKVT ALSEVSQKLG
     EKVYADMQAK AGEQGAAGAA GAGAQQQAQP QDDNVVDAEF KEVNDKK