ID   DNAK_YERE8              Reviewed;         635 AA.
AC   A1JJD5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=YE0609;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(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; AM286415; CAL10723.1; -; Genomic_DNA.
DR   RefSeq; WP_011815538.1; NC_008800.1.
DR   RefSeq; YP_001004963.1; NC_008800.1.
DR   AlphaFoldDB; A1JJD5; -.
DR   SMR; A1JJD5; -.
DR   STRING; 393305.YE0609; -.
DR   PRIDE; A1JJD5; -.
DR   EnsemblBacteria; CAL10723; CAL10723; YE0609.
DR   KEGG; yen:YE0609; -.
DR   PATRIC; fig|393305.7.peg.704; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000642; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059699"
FT   REGION          602..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..635
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   635 AA;  68877 MW;  9D0FD8A194ED1661 CRC64;
     MGKIIGIDLG TTNSCVAIMD GTKARVLENS EGDRTTPSII AYTQDGETLV GQPAKRQAVT
     NPQNTLFAIK RLIGRRFQDE EAQRDKDIMP YKIIAADNGD AWLEVKGQKI 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 DKTAIEDAVK ALEAALKSED KAEIEAKTQA LVQVSGKLLE
     MAQQQAAAGG DAGDTSAKKE DDVVDAEFEE VKDKK