ID   DNAK_BACFN              Reviewed;         639 AA.
AC   Q5LG30;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=BF1189;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH06911.1; -; Genomic_DNA.
DR   RefSeq; WP_005785809.1; NC_003228.3.
DR   AlphaFoldDB; Q5LG30; -.
DR   SMR; Q5LG30; -.
DR   STRING; 272559.BF9343_1130; -.
DR   EnsemblBacteria; CAH06911; CAH06911; BF9343_1130.
DR   GeneID; 66329839; -.
DR   KEGG; bfs:BF9343_1130; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006731; 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   CHAIN           1..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225937"
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