ID   DNAK_ACIC1              Reviewed;         618 AA.
AC   A0LWS7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, 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=Acel_2115;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK53887.1; -; Genomic_DNA.
DR   RefSeq; WP_011720950.1; NC_008578.1.
DR   AlphaFoldDB; A0LWS7; -.
DR   SMR; A0LWS7; -.
DR   STRING; 351607.Acel_2115; -.
DR   PRIDE; A0LWS7; -.
DR   EnsemblBacteria; ABK53887; ABK53887; Acel_2115.
DR   KEGG; ace:Acel_2115; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008221; 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; 2.
DR   Pfam; PF00012; HSP70; 2.
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..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059497"
FT   REGION          492..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   618 AA;  66202 MW;  DA393CB351B8A067 CRC64;
     MARAVGIDLG TTNSVIAVLE GGEPTVIPNA EGSRTTPSVV AFAKNGEVLV GEVAKRQAVT
     NAERTIRSVK RHMGTNWTID IDGKKYTPQE ISARILMKLK RDAEAYLGEQ ISDAVITVPA
     YFNDAQRQAT KEAGQIAGLN VLRIINEPTA AALAYGLDKG EKEQTILVFD LGGGTFDVSL
     LEIGEGIVEV KATSGDTHLG GDDWDQRIVD HLVTTFKNQH GIDLSKDKMA MQRLKEAAER
     AKIELSSAME TTINLPYITA SSEGPLHLEV KLTRSEFQRM TADLLERCKG PFNQAIKDAG
     ITVNQIDHVI LVGGSTRMPA VVDLVRELTG GKEPNKGVNP DEVVAVGACL QAGVLKGEVK
     DVLLLDVTPL SLGIETKGGV FTKLIERNTT IPTRRSEIFT TAEDNQPSVQ IQVYQGEREI
     AAYNKKLGMF ELTGLPPAPR GVPQIEVTFD IDANGIVHVS AKDLATGKEQ SMTITGGSAL
     PKEEIERMMR DAEAHAEEDR RRREEAEARN QADTLIYQTE KFLRENADKV PAAEKANVET
     AIANLKKAME GSDVTAIRSA TEQLATESQK LGAAMYAATQ AAAGGSSGSA TGATGSASGS
     AGKDDEVVDA EIVDEGEK