DNAK_DECAR
ID DNAK_DECAR Reviewed; 645 AA.
AC Q47HK2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Daro_0923;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ45679.1; -; Genomic_DNA.
DR RefSeq; WP_011286688.1; NC_007298.1.
DR AlphaFoldDB; Q47HK2; -.
DR SMR; Q47HK2; -.
DR STRING; 159087.Daro_0923; -.
DR PRIDE; Q47HK2; -.
DR EnsemblBacteria; AAZ45679; AAZ45679; Daro_0923.
DR KEGG; dar:Daro_0923; -.
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..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225955"
FT REGION 604..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..645
FT /note="Basic and acidic residues"
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 645 AA; 69333 MW; 8F3A1A3C5D49F233 CRC64;
MGKIIGIDLG TTNSCVAIME GGQPKVIENA EGARTTPSII GYTEDGEILC GAPAKRQAVT
NPKNTLYAVK RLIGRRFEEK EVQKDISLMP FKIVKADNGD AWVEARDKKI APPQVSAEVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
MDKTSKSDRK IAVYDLGGGT FDISIIEIAN VDGETQFEVL ATNGDTFLGG EDFDQRLIDY
IIDEFKKESG VNLKADVLAL QRLKEAAEKA KIELSSSQQT EVNLPYITAD ASGPKHLALK
ITRAKFESLV DELIERTMAP CVTALKDAGC KISDIDDIIL VGGQSRMPKV QEKVKEIFGK
EPRKDVNPDE AVAVGAAIQG GVLQGEVKDV LLLDVTPLSL GIETLGGIMT KLIQKNTTIP
TKASQTFSTA DDNQAAVTIH VLQGEREVAS GNKSLGQFNL EGIPPAPRGT PQIEVIFDID
ANGIMHVTAK DKATGKENKI TIKANSGLSE AEIQAMVKDA ELHAEEDKKA HELADARNQA
DGMVHMVKKS LTEYGDKLDA SEKAAIEAAI KDVEDVLRDG DKETITAKTE ALSAAAQKLG
EKMYAQQQAE GAAAGATGQQ AEAGEKTVEG DVVDAEFTEV NKDKK