ID   DNAK_MANHA              Reviewed;         631 AA.
AC   O52064;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
OS   Mannheimia haemolytica (Pasteurella haemolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=75985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A1;
RA   Al S.L., Lo R.Y.C.;
RT   "The dnaK and dnaJ chaperone genes of Pasteurella haemolytica A1.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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; AF017730; AAB94554.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52064; -.
DR   SMR; O52064; -.
DR   STRING; 75985.WC39_01750; -.
DR   PRIDE; O52064; -.
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..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078506"
FT   REGION          601..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   631 AA;  67980 MW;  4DE9FEC3A36B4E6F CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGARTTPSII AYTDKETLVG QPAKRQAITN
     PKNTLFAIKR LIGRRFTDAE VQRDIEIMPF EISKADNGDA WVTVKGDKLA PPQISAEILK
     KMKKTAEDFL GEPVTEAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGL
     DSKKENQTIA VYDLGGGTFD ISIIEIDNFD GEQTFEVRAT NGDTHLGGED FDNRVINYLV
     EEFKKQGVDL RNDPMAMQRV KEAAEKAKIE LSSAQETEVN LPYITADATG PKHLNIKVTR
     AKLESLVEDL VNRSLEPLKT ALADAGLSVG DINDVILVGG QTRMPLVQKK VADFFGKTRK
     DVNPDEAVMA IGAAVQGGVL SGSVTDVLLL DVTPLSLGIE TMGGVMTTLI EKNTTIPTKK
     SQVFSTAEDN QSAVTIHVLQ GERKRAADNK SLGQFNLEGI NPAPRGMPQI EVTFDIDANG
     IINVSAKDKN TGKEQQIKIQ ASSGLSDAEV EQMVRDAEAN AEADKKFEEL VQVCNQADGI
     AHATRKQITE AGDALNADDK AKIEAAISEL ETAAKGEDKA EIEAKIEALI KASEPLMLAA
     QAKAQGGEQP QQSQKDDGVV DAEFEEVKDN K