ID   DNAK_CELJU              Reviewed;         640 AA.
AC   B3PF33;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=CJA_3347;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84909.1; -; Genomic_DNA.
DR   RefSeq; WP_012488923.1; NC_010995.1.
DR   AlphaFoldDB; B3PF33; -.
DR   SMR; B3PF33; -.
DR   STRING; 498211.CJA_3347; -.
DR   PRIDE; B3PF33; -.
DR   EnsemblBacteria; ACE84909; ACE84909; CJA_3347.
DR   KEGG; cja:CJA_3347; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001036; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119683"
FT   REGION          606..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..640
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   640 AA;  68108 MW;  73FF2F49D41A2BED CRC64;
     MGKIIGIDLG TTNSCVSILE GGAPKVIENA EGDRTTPSII AFTNDGEILV GQSAKRQAVT
     NPHNTLFAVK RLIGRKFKDD VVQKDISMVP YKIVAADNGD AWVEVKGEKK APPQISAEVL
     KKMKKTAEDY LGEKVTEAVI TVPAYFNDSQ RQATKDAGKI AGLDVKRIIN EPTAAALAYG
     LDKGKGDHTI AVYDLGGGTF DISIIEIADV DGEHQFEVLS TNGDTFLGGE DFDMRLIEFL
     ADSFKKDTGI DLHNDPLALQ RLKEAAEKAK IELSSSQQTE VNLPYITADA TGPKHLVVKL
     TRAKLESLVE DLVNKSLEPV KQAIKDSGKS ISDIDDVILV GGQTRMPLVQ KAVADYFGKE
     PRKDVNPDEA VAIGAAIQGA VLAGDVKDVL LLDVTPLTLG IETMGGVATP LIEKNTTIPT
     KKSQVFSTAD DNQTAVTIHV VQGERKQASQ NKSLGRFDLA DIPPAPRGMP QIEVTFDIDA
     NGILNVSAKD KATGKEQSIV IKASSGLSDD EIQKMVKDAE ANAEADRKFA ELVGARNTLE
     GLIHATQKTV KEAGDKATAD EKAAIDAAVK EAEEAVKGDD LARIEAATTK LTEASSSLAQ
     KLYAEQQAAG AGAQQADGTG KAADDGVVDA EFEEVKEDNK