ID   DNAK_BURMA              Reviewed;         650 AA.
AC   Q62HD5; Q4PPC1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BMA2326;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RA   Amemiya K., Meyers J.L., Norris S.L., DeShazer D., Waag D.M.;
RT   "Heat-shock proteins GroEL and DnaK are immunogenic in a patient and mice
RT   infected with Burkholderia mallei.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; DQ061984; AAY63995.1; -; Genomic_DNA.
DR   EMBL; CP000010; AAU49784.1; -; Genomic_DNA.
DR   RefSeq; WP_004194034.1; NC_006348.1.
DR   RefSeq; YP_103885.1; NC_006348.1.
DR   AlphaFoldDB; Q62HD5; -.
DR   SMR; Q62HD5; -.
DR   STRING; 243160.BMA2326; -.
DR   EnsemblBacteria; AAU49784; AAU49784; BMA2326.
DR   GeneID; 56594684; -.
DR   KEGG; bma:BMA2326; -.
DR   PATRIC; fig|243160.12.peg.2394; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000006693; Chromosome 1.
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_0000225944"
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"
FT   CONFLICT        79
FT                   /note="E -> G (in Ref. 1; AAY63995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="G -> C (in Ref. 1; AAY63995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="A -> S (in Ref. 1; AAY63995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="A -> V (in Ref. 1; AAY63995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="A -> T (in Ref. 1; AAY63995)"
FT                   /evidence="ECO:0000305"
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