DNAK_BRUAB
ID DNAK_BRUAB Reviewed; 637 AA.
AC Q57AD7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BruAb1_2100;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(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; AE017223; AAX75397.1; -; Genomic_DNA.
DR RefSeq; WP_002969217.1; NC_006932.1.
DR AlphaFoldDB; Q57AD7; -.
DR SMR; Q57AD7; -.
DR EnsemblBacteria; AAX75397; AAX75397; BruAb1_2100.
DR GeneID; 45125373; -.
DR KEGG; bmb:BruAb1_2100; -.
DR HOGENOM; CLU_005965_3_0_5; -.
DR OMA; ISIKRHM; -.
DR PRO; PR:Q57AD7; -.
DR Proteomes; UP000000540; 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_0000225943"
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:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 637 AA; 68194 MW; C659ABDE5529B91E 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 GLSDADIEKM VKDAEANAEA DKKRRESVEA KNQAESLVHS
TEKSLAEYGD KVSADDKKAI EDAIAALKTS LEGEDAEDIK AKTQALAEVS MKLGQAMYEA
AQAAEGAGAE GGEQASSSKD DVVDADYEEI DDNKKSS