ID   DNAK_BURCE              Reviewed;         650 AA.
AC   P42373;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
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;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7528198; DOI=10.1128/jb.176.24.7748-7753.1994;
RA   Falah M., Gupta R.S.;
RT   "Cloning of the hsp70 (dnaK) genes from Rhizobium meliloti and Pseudomonas
RT   cepacia: phylogenetic analyses of mitochondrial origin based on a highly
RT   conserved protein sequence.";
RL   J. Bacteriol. 176:7748-7753(1994).
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}.
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DR   EMBL; L36603; AAC41409.1; -; Genomic_DNA.
DR   PIR; A55551; A55551.
DR   AlphaFoldDB; P42373; -.
DR   SMR; P42373; -.
DR   STRING; 292.DM42_1086; -.
DR   eggNOG; COG0443; Bacteria.
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_0000078436"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   650 AA;  69741 MW;  EC292237239294D2 CRC64;
     MGKIIGIDLG TTNSCVAIME GNQVKVIENS EGTRTTPSII AYMDDNEVLV GAPAKRQSVT
     NPKNTLFAVK RLIGRRFEEK EVQKDIGLMP YSIIKADNGD AWVEGHGEKL MAPPQVSAEA
     VRKMKKTAED YLGEPVTEAV ITVPAYFNDS QRQATKDAGR IAGLEVKRII NEPTAAALAF
     GLDKAEKGDR KIAVYDLGGG TFDVSIIEIA DVDGEMQFEV LSTNGDTFLG GEDFDQRIID
     YIIGEFKKEQ GVDLSKDVLA LQRLKEAAEK AKIELSSSQQ TEINLPYITA DASGPKHLNL
     KITRAKLEAL VEDLVERTIE PCRIAIKDAG VKVSDIDDVI LVGGQTRMPK VMEKVKEFFG
     KDPRRDVNPD EAVAVGAAIQ GQVLSGDRKD VLLLDVTLSL GIETVGGVMT KMISKNTTIP
     TKHAQVYSTA DDNQGAVTIK VFQGEREMAA GNKLLGEFNL EGIPPAPRGV PQIEVTFDID
     ANGILHVGAK DKATGKENKI TIKANSGLSE AEIDQMIKDA EANAAEDHNV RELADSRNQG
     DALVHSTKKA LTEYGDKLDA GEKEALEASL KSLEEVLKDT SADKAAIDAK VEELGKVSQK
     LGEKMYADMQ AQQAGAAGAA GAAEGAAHAG GAQQAADDVV DAEFKEVKKD