DNAK_CUPNH
ID DNAK_CUPNH Reviewed; 650 AA.
AC Q0K757;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=H16_A3089;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ94164.1; -; Genomic_DNA.
DR RefSeq; WP_010815035.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K757; -.
DR SMR; Q0K757; -.
DR STRING; 381666.H16_A3089; -.
DR PRIDE; Q0K757; -.
DR EnsemblBacteria; CAJ94164; CAJ94164; H16_A3089.
DR GeneID; 57645214; -.
DR KEGG; reh:H16_A3089; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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..650
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059639"
FT REGION 612..650
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 650 AA; 69907 MW; 48D90FCE3E4E828E CRC64;
MGKIIGIDLG TTNSCVAILE GNTPKVIENS EGARTTPSII AYMEDGEILV GAPAKRQAVT
NPRNTLYAVK RLIGRKFEEK EVQKDIGLMP YSIVKADNGD AWVSVRDQKL APPQVSAEVL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
MDKNEKGDRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
IISEFKKDQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
MTRAKLESLV EELITRTIEP CRIAIKDAGV KVSDIDDVIL VGGMTRMPKV QEQVKEFFGK
EARKDVNPDE AVAVGAAIQG SVLSGDRTDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKHAQVFSTA DDNQPAVTIK VFQGEREMAS GNKLLGEFNL EGIPPAARGT PQIEVSFDID
ANGILHVGAK DKATGKENRI TIKANSGLSE DEIQRMVKDA EANAEEDKKA RELADARNQA
DALIHSTKKA LTEYGDKLEA GEKEKIEAAI KELEDAARGG DKAEIDAKVN ALSEVSQKLG
EKVYADMQAK AGEGATAGAA AGAGAAGGQQ AQPQDDNVVD AEFKEVNDKK