DNAK_BRUO2
ID DNAK_BRUO2 Reviewed; 637 AA.
AC Q05981; A5VT77;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=BOV_2041;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1459952; DOI=10.1128/jb.174.24.8036-8042.1992;
RA Cellier M.F.M., Teyssier J., Nicolas M., Liautard J.P., Marti J.,
RA Sri Widada J.;
RT "Cloning and characterization of the Brucella ovis heat shock protein DnaK
RT functionally expressed in Escherichia coli.";
RL J. Bacteriol. 174:8036-8042(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; M95799; AAC36132.1; -; Genomic_DNA.
DR EMBL; CP000708; ABQ61277.1; -; Genomic_DNA.
DR PIR; A47042; A47042.
DR RefSeq; WP_002969217.1; NC_009505.1.
DR AlphaFoldDB; Q05981; -.
DR SMR; Q05981; -.
DR EnsemblBacteria; ABQ61277; ABQ61277; BOV_2041.
DR GeneID; 45125373; -.
DR KEGG; bov:BOV_2041; -.
DR HOGENOM; CLU_005965_3_0_5; -.
DR OMA; ISIKRHM; -.
DR PhylomeDB; Q05981; -.
DR PRO; PR:Q05981; -.
DR Proteomes; UP000006383; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078431"
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"
FT CONFLICT 48..49
FT /note="RL -> GV (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="I -> L (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="E -> D (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="I -> T (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..300
FT /note="KF -> NV (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..310
FT /note="LVQR -> AVHA (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="K -> E (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="EV -> KC (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 438..442
FT /note="GEREM -> ASVKL (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="P -> R (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..489
FT /note="KGTG -> GGVP (in Ref. 1; AAC36132)"
FT /evidence="ECO:0000305"
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
