ID   DNAK_HAEDU              Reviewed;         634 AA.
AC   P48209;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 134.
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=HD_0189;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Parsons L.M.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; U25996; AAA67298.1; -; Genomic_DNA.
DR   EMBL; AE017143; AAP95182.1; -; Genomic_DNA.
DR   RefSeq; WP_010944236.1; NC_002940.2.
DR   AlphaFoldDB; P48209; -.
DR   SMR; P48209; -.
DR   STRING; 233412.HD_0189; -.
DR   EnsemblBacteria; AAP95182; AAP95182; HD_0189.
DR   KEGG; hdu:HD_0189; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001022; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078467"
FT   REGION          599..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   634 AA;  68549 MW;  434AD3C505CD0EF0 CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKPRVLENA EGARTTPSII AYTDKETLVG QPAKRQAITN
     PKNTLFAIKR LIGRRFTDNE VQRDIEIMPF EIAKADNGDA WVNVKGDKLA PPQISAEVLK
     KMKKTAEDFL GEPVTEAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
     DSKKENQIIA VYDLGGGTFD ISIIEIDNFD GEQTFEVRAT NGDTHLGGED FDNRVINYLV
     EEFQKEQGVD LRNDPMAMQR VKEAAEKAKI ELSSAQETEV NLPYITADAT GPKHLNIKVT
     RAKLEALVED LVSRSLEPLK TALADAGLSV SEINDVILVG GQTRMPLVQK KVADFFGKEP
     RKDVNPDEAV AIGAAVQGGV LAGDVTDVLL LDVTPLSLGI ETMGGVMTSL IEKNTTIPTK
     KSQVFSTAED NQSAVTIHVL QGERKRAADN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN
     GIINVSAKDK NTGKEQQIKI QASSGLSDEE VEQMVRDAEA NAESDRQFEE LVQTRNQADS
     IAHATRKQIS EAGDALTAED KAKIETALAE LETAAKGEDK AEIEAKIEAV IKASEPLMQA
     AQAKAQTNQA GEQQSSAKDD SVVDAEFEEV KENK