DNAK_BURM7
ID DNAK_BURM7 Reviewed; 650 AA.
AC A3MN99;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=BMA10247_2206;
OS Burkholderia mallei (strain NCTC 10247).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10247;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000548; ABO05674.1; -; Genomic_DNA.
DR RefSeq; WP_004194034.1; NZ_CP007802.1.
DR AlphaFoldDB; A3MN99; -.
DR SMR; A3MN99; -.
DR GeneID; 56594684; -.
DR KEGG; bmaz:BM44_1036; -.
DR KEGG; bmn:BMA10247_2206; -.
DR PATRIC; fig|320389.8.peg.1157; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000002284; 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..650
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059520"
FT REGION 611..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 650 AA; 69702 MW; A386275A28E174D5 CRC64;
MGKIIGIDLG TTNSCVAIME GNQVKVIENS EGARTTPSII AYMDDNEVLV GAPAKRQSVT
NPKNTLFAVK RLIGRRFEEK EVQKDIGLMP YAIIKADNGD AWVEAHGEKL APPQVSAEVL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
LDKAEKGDRK IAVYDLGGGT FDVSIIEIAD VDGEMQFEVL STNGDTFLGG EDFDQRIIDY
IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
VTRAKLEALV EDLVERTIEP CRTAIKDAGV KVSDIDDVIL VGGQTRMPKV QEKVKEFFGK
EPRRDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMINKNTTIP
TKHAQVYSTA DDNQGAVTIK VFQGEREMAA GNKLLGEFNL EGIPPAPRGV PQIEVTFDID
ANGILHVGAK DKATGKENKI TIKANSGLSE AEIEKMVKDA EANAAEDHKL RELAESRNQG
DALVHSTKKA LTEYGDKLEA GEKEKIEAAL KELEDVLKNA SSDKAAIDAK VEAVATASQK
LGEKMYADMQ AQQAGAAGAA GAAAEGASAQ GGAQPADDVV DADFKEVKKD