ID   DNAK_PASMU              Reviewed;         634 AA.
AC   P57870;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=PM0736;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AE004439; AAK02820.1; -; Genomic_DNA.
DR   RefSeq; WP_010906826.1; NC_002663.1.
DR   AlphaFoldDB; P57870; -.
DR   SMR; P57870; -.
DR   STRING; 747.DR93_1567; -.
DR   PRIDE; P57870; -.
DR   EnsemblBacteria; AAK02820; AAK02820; PM0736.
DR   KEGG; pmu:PM0736; -.
DR   PATRIC; fig|272843.6.peg.744; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000809; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078507"
FT   REGION          599..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   634 AA;  68431 MW;  060F34200E5ACB20 CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGDRTTPSII AYTQDNETLV GQPAKRQAVT
     NPKNTLFAIK RLIGRRFQDE EVQRDVSIMP FEIVAADNGD AWVGVKGEKM APPQISAEVL
     KKMKKTAEDF LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKGQGNKTI AVYDLGGGTF DLSIIEIDEV GGEKTFEVLS TNGDTHLGGE DFDNRVINYL
     VDEFKKEQGV DLRNDPLAMQ RLKEAGEKAK IELSSAQQTD VNLPYITADA TGPKHLNIKL
     TRAKLESLVE DLVSRSLEPV KIALADAGLS VSQIDDVILV GGQTRMPLVQ QKVEAFFGKA
     PRKDVNPDEA VAIGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTT LIEKNTTIPT
     KKSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLE GINPAPRGMP QIEVTFDIDA
     DGIIHVSAKD KGTNKEQKIT IKASSGLTDE EIQQMVRDAE ANAEADRKFE ELVQARNQAD
     HLVHGTRKQL SEVGDKLSAE DKAPIEKAVA DLEAAAKGED KAEIETKVQA LIQVSEKLMQ
     AAQPQPEAQA QQAQSGKSND DVVDAEFEEV KDNK