ID   DNAK_BRUME              Reviewed;         637 AA.
AC   Q8YE76;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=BMEI2002;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL53183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL53183.1; ALT_INIT; Genomic_DNA.
DR   PIR; AD3502; AD3502.
DR   RefSeq; WP_041594641.1; NC_003317.1.
DR   AlphaFoldDB; Q8YE76; -.
DR   SMR; Q8YE76; -.
DR   STRING; 224914.BMEI2002; -.
DR   PRIDE; Q8YE76; -.
DR   EnsemblBacteria; AAL53183; AAL53183; BMEI2002.
DR   GeneID; 29594878; -.
DR   KEGG; bme:BMEI2002; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; Q8YE76; -.
DR   PRO; PR:Q8YE76; -.
DR   Proteomes; UP000000419; 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; 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_0000078430"
FT   REGION          516..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        516..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:0000250"
SQ   SEQUENCE   637 AA;  68212 MW;  2759ABA5340BB436 CRC64;
     MAKVIGIDMG 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 GLSDADIEKM VKDAEANAEA DKKRRESVEA KNQAESLVHS
     TEKSLAEYGD KVSADDKKAI EDAIAALKTS LEGEDAEDIK AKTQALAEVS MKLGQAMYEA
     AQAAEGAGAE GGEQASSSKD DVVDADYEEI DDNKKSS