ID   DNAK_CUPMC              Reviewed;         648 AA.
AC   O33522; Q1LJ81;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 132.
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=Rmet_2922;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Talbi S., van der Lelie D.;
RT   "Construction and characterization of a DnaK mutant of Ralstonia eutropha
RT   strain CH34.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AJ001727; CAA04955.1; -; Genomic_DNA.
DR   EMBL; CP000352; ABF09795.1; -; Genomic_DNA.
DR   RefSeq; WP_011517467.1; NC_007973.1.
DR   AlphaFoldDB; O33522; -.
DR   SMR; O33522; -.
DR   STRING; 266264.Rmet_2922; -.
DR   PRIDE; O33522; -.
DR   EnsemblBacteria; ABF09795; ABF09795; Rmet_2922.
DR   KEGG; rme:Rmet_2922; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002429; 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.
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..648
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078406"
FT   REGION          612..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        119..120
FT                   /note="VL -> AV (in Ref. 1; CAA04955)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..151
FT                   /note="SQR -> AQC (in Ref. 1; CAA04955)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="K -> R (in Ref. 1; CAA04955)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="L -> C (in Ref. 1; CAA04955)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553..581
FT                   /note="EYGEKLEAGEKEKIEAAIKDLEDAARGGD -> RVRREARSWREGKDRSRDQ
FT                   GPGRRRPRVN (in Ref. 1; CAA04955)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        623..648
FT                   /note="GGAQQQAQPQDDNVVDAEFKEVNDKK -> RFSSRPSRRRQRVGCRVQGSER
FT                   QEVIGDG (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   648 AA;  69787 MW;  0E962FFF93C6CCA4 CRC64;
     MGKIIGIDLG TTNSCVSILE GNTPKVIENS EGARTTPSII AYMEDGEILV GAPAKRQAVT
     NPRNTLYAVK RLIGRKFEEK EVQKDIGLMP YAIVKADNGD AWVGVRDQKL APPQVSAEVL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     MDKNEKGDRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
     ITRAKLEALV EELITRTIEP CRTAIKDAGV KVSDIDDVIL VGGMTRMPKV QEQVREFFGK
     EARKDVNPDE AVAVGAAIQG SVLSGDRTDV LLLDVTPLSL GIETLGGVMT KMINKNTTIP
     TKHAQVFSTA DDNQPAVTIK VYQGEREMAT GNKMLGEFNL EGIAPAPRGT PQIEVSFDID
     ANGILHVGAK DKATGKENRI TIKANSGLSE DEIQRMVKDA EANAEEDKRA RELADARNQA
     DALIHSTRKA LGEYGEKLEA GEKEKIEAAI KDLEDAARGG DKAEIDAKVN ALSEASQKLG
     EKVYADMQAQ AGEGAAAGAG AAGGAQQQAQ PQDDNVVDAE FKEVNDKK