ID   DNAK_BACFR              Reviewed;         639 AA.
AC   Q64X01;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BF1225;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD47975.1; -; Genomic_DNA.
DR   RefSeq; WP_005785809.1; NC_006347.1.
DR   RefSeq; YP_098509.1; NC_006347.1.
DR   AlphaFoldDB; Q64X01; -.
DR   SMR; Q64X01; -.
DR   STRING; 295405.BF1225; -.
DR   EnsemblBacteria; BAD47975; BAD47975; BF1225.
DR   GeneID; 66329839; -.
DR   KEGG; bfr:BF1225; -.
DR   PATRIC; fig|295405.11.peg.1212; -.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002197; 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   Stress response.
FT   CHAIN           1..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225936"
FT   REGION          600..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   639 AA;  68595 MW;  9F4898509D826BEE CRC64;
     MGKIIGIDLG TTNSCVSVFE GNEPVVIANS EGKRTTPSIV AFVDGGERKV GDPAKRQAIT
     NPTRTIFSIK RFMGENWDQV QKEIARVPYK VVKGDNNTPR VDIDGRLYTP QEISAMILQK
     MKKTAEDYLG QEVTEAVITV PAYFSDSQRQ ATKEAGQIAG LEVKRIVNEP TAAALAYGLD
     KAHKDMKIAV FDLGGGTFDI SILEFGGGVF EVLSTNGDTH LGGDDFDQVI IDWLVQEFKN
     DEGADLTQDP MAMQRLKEAA EKAKIELSSS TSTEINLPYI MPVGGVPKHL VKTLTRAKFE
     SLAHNLIQAC LEPCKKAMQD AGLSNSDIDE VILVGGSSRI PAVQKLVEDF FGKTPSKGVN
     PDEVVAVGAA VQGAVLTDEI KGVVLLDVTP LSMGIETLGG VMTKLIDANT TIPARKSETF
     STAADNQTEV TIHVLQGERP MAAQNKSIGQ FNLTGIAPAR RGVPQIEVTF DIDANGILKV
     SAKDKATGKE QAIRIEASSG LSKEEIEKMK AEAEANAEAD KKEREKIDKL NQADSLIFQT
     ETQLKELGDK LPADKKAPIE AALQKLKDAH KAQDMTTIDS AMAELNTAFQ AASAEMYAQS
     GAQGGAQAGP DMNAGQSNAG QNNGKQDDNV QDADFEEVK