ID   DNAK_PSEP1              Reviewed;         611 AA.
AC   A5W9A3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Pput_4593;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ80713.1; -; Genomic_DNA.
DR   RefSeq; WP_012053754.1; NC_009512.1.
DR   AlphaFoldDB; A5W9A3; -.
DR   SMR; A5W9A3; -.
DR   STRING; 351746.Pput_4593; -.
DR   EnsemblBacteria; ABQ80713; ABQ80713; Pput_4593.
DR   KEGG; ppf:Pput_4593; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
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..611
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059635"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   611 AA;  65492 MW;  04B7D07A26056F4F CRC64;
     MGKIIGIDLG TTNSCVSILE NGNVKVIENA EGARTTPSIV AYANDGEILV GQSAKRQAVT
     NPHNTLFAVK RLIGRRFEED VVQKDIKLVP YKIVKANNGD AWVEAAGKEM APPQISAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     MDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDMRLIDYL
     VDEFKKESGM DLKNDPLALQ RLKEAAEKAK IELSSAQSTD VNLPYITADA TGPKHLNVKI
     SRAKLESLVE DLVKRTIEPC RIALKDAGID ASKIDDVILV GGQTRMPLVQ KEVADFFGKE
     ARKDVNPDEA VAMGAAIQGA VLAGDVKDVL LLDVSPLTLG IETMGGVMTA LIEKNTTIPT
     KKSQVFSTAD DNQSAVTIHV LQGERKQAAQ NKSLGKFDLA DIPPAPRGVP QIEVTFDIDA
     NGILHVGAKD KATGKTQSIV IKANSGLSDE EIERMVRDAE ANAEEDRKFE ELAAARNQGD
     ALVHSTRKMV ADAGDKVTAE EKTAIEAAVV ALEAAVKGDD KAAIDAKVEE LSKVSAPVAQ
     KMYAEQSAEQ P