ID   DNAK_YERPS              Reviewed;         636 AA.
AC   Q66ET0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=YPTB0611;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19851.1; -; Genomic_DNA.
DR   RefSeq; WP_002209248.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66ET0; -.
DR   SMR; Q66ET0; -.
DR   ChEMBL; CHEMBL1741204; -.
DR   EnsemblBacteria; CAH19851; CAH19851; YPTB0611.
DR   GeneID; 66842968; -.
DR   KEGG; ypo:BZ17_1945; -.
DR   KEGG; yps:YPTB0611; -.
DR   PATRIC; fig|273123.14.peg.2069; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001011; 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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226033"
FT   REGION          603..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
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   636 AA;  69025 MW;  0356EAE0BF100319 CRC64;
     MGKIIGIDLG TTNSCVAIMD GTKARVLENS EGDRTTPSII AYTQDGETLV GQPAKRQAVT
     NPQNTLFAIK RLIGRRFQDE EAQRDKDIMP YKIIAADNGD AWLEVKGQKM APPQISAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKEVGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
     VEEFKKDQGM DLRTDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADG SGPKHMNIKV
     TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIQDVILV GGQTRMPMVQ KKVADFFGKE
     PRKDVNPDEA VAIGAAVQGG VLSGEVKDVL LLDVTPLSLG IETMGGVMTP LITKNTTIPT
     KHSQVFSTAE DNQSAVTIHV LQGERKRAQD NKSLGQFNLD GIQPAPRGMA QIEVTFDIDA
     DGILHVSAKD KNTGREQKIT IKASSGLNEE EIQKMVRDAE ANAEADRKFE ELVQTRNQAD
     HLIHGTRKQL EEAGDKLPAE DKTAIEEAMK GLEAALKGED KAEIEAKTQA LVQVSGKLLE
     MAQQQQAAAG GDAGDTSAKK EDDVVDAEFE EVKDKK