DNAK_PSEE4
ID DNAK_PSEE4 Reviewed; 641 AA.
AC Q1IF59;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-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=PSEEN0778;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(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; CT573326; CAK13695.1; -; Genomic_DNA.
DR RefSeq; WP_011532126.1; NC_008027.1.
DR AlphaFoldDB; Q1IF59; -.
DR SMR; Q1IF59; -.
DR STRING; 384676.PSEEN0778; -.
DR PRIDE; Q1IF59; -.
DR EnsemblBacteria; CAK13695; CAK13695; PSEEN0778.
DR KEGG; pen:PSEEN0778; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000658; 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 Stress response.
FT CHAIN 1..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059633"
FT REGION 602..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 68634 MW; AF4F642E999981EC CRC64;
MGKIIGIDLG TTNSCVSVLE NGTAKVIENA EGARTTPSII AYANDGEILV GQSAKRQAVT
NPHNTLFAVK RLIGRRFDEE VVQKDIKLVP YKIVKASNGD AWVQASGKDM APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDMRLIDYL
VDEFKKESGM DLKNDPLALQ RLKEAAEKAK IELSSAQSTD VNLPYITADA TGPKHLNVKI
SRAKLEALVE DLVTRTIEPC RIALKDAGID ASKIDDVILV GGQTRMPMVQ KAVADFFGKE
ARKDVNPDEA VAMGAAIQGA VLAGDVKDVL LLDVSPLTLG IETMGGVMTA LIEKNTTIPT
KKSQVFSTAD DNQGAVTIHV LQGERKQASQ NKSLGKFDLA DIPPAPRGVP QIEVTFDIDA
NGILHVGAKD KATGKAQSIV IKANSGLSDE EVERMVRDAE ANAEEDRKFE ELAAARNQGD
ALVHSTRKMV ADAGDKVTAE EKTAIEAAVV ALEAAVKGDD KAAIDAKVEE LSKVSAPVAQ
KMYAEQQAEQ PQGGAQQAEP EAKHDDVVDA EFEEVKDNNK Q