ID   DNAK_BRUSU              Reviewed;         637 AA.
AC   Q8FXX2; G0K973;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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};
GN   OrderedLocusNames=BR2125, BS1330_I2119;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN31015.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM19432.1; -; Genomic_DNA.
DR   RefSeq; WP_004691170.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8FXX2; -.
DR   SMR; Q8FXX2; -.
DR   EnsemblBacteria; AEM19432; AEM19432; BS1330_I2119.
DR   GeneID; 45053050; -.
DR   GeneID; 55591691; -.
DR   KEGG; bms:BR2125; -.
DR   KEGG; bsi:BS1330_I2119; -.
DR   PATRIC; fig|204722.21.peg.687; -.
DR   HOGENOM; CLU_005965_3_0_5; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; Q8FXX2; -.
DR   PRO; PR:Q8FXX2; -.
DR   Proteomes; UP000007104; Chromosome I.
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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078432"
FT   REGION          514..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..637
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:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   637 AA;  68208 MW;  C082ABDE53F2BBD5 CRC64;
     MAKVIGIDLG TTNSCVAVMD GKNAKVIENA EGARTTPSII AFTDGDERLA GQPAKRQAVT
     NPEGTLFAVK RLIGRRYDDP MVTKDKDLVP YKIVKGDNGD AWVEVHGKKY SPSQISAMIL
     QKMKETAESY LGETVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKSEGKTIA VYDLGGGTFD VSVLEIGDGV FEVKSTNGDT FLGGEDFDIR LVEYLVAEFK
     KESGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADQTGPKH LAIKLSRAKF
     ESLVDDLVQR TVEPCKAALK DAGLKAGEID EVVLVGGMTR MPKIQEVVKA FFGKEPHKGV
     NPDEVVAMGA AIQGGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQT
     FSTAEDNQSA VTIRVFQGER EMAADNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVN
     VSAKDKGTGK EHQIRIQASG GLTDADIEKM VKDAEANAEA DKKRRESVEA KNQAESLVHS
     TEKSLAEYGD KVSADDKKAI EDAIAALKTS LEGEDAEDIK AKTQALAEVS MKLGQAMYEA
     AQAAEGAGAE GGEQASSSKD DVVDADYEEI DDNKKSS