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 27-MAR-2024, entry version 140. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; hdu:HD_0189; -. DR eggNOG; COG0443; Bacteria. DR HOGENOM; CLU_005965_2_1_6; -. DR OrthoDB; 9766019at2; -. 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; 3.30.420.40; -; 2. 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 NCBIfam; TIGR02350; prok_dnaK; 1. DR PANTHER; PTHR19375:SF541; CHAPERONE PROTEIN DNAK; 1. DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1. DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 //