ID   DNAK_BRECH              Reviewed;         610 AA.
AC   Q9LCQ5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Brevibacillus choshinensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPD31;
RX   PubMed=9748507; DOI=10.1016/s0167-4838(98)00108-3;
RA   Tokunaga H., Yamakawa M., Mizukami M., Takagi H., Tokunaga M.;
RT   "Molecular cloning of the dnaK locus, and purification and characterization
RT   of a DnaK protein from Bacillus brevis HPD31.";
RL   Biochim. Biophys. Acta 1387:65-79(1998).
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; AB009842; BAA90473.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LCQ5; -.
DR   SMR; Q9LCQ5; -.
DR   STRING; 54911.AN963_03935; -.
DR   PRIDE; Q9LCQ5; -.
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; 2.
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..610
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078429"
FT   REGION          581..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   610 AA;  65482 MW;  BFECEE129379D50A CRC64;
     MSRVIGIDLG TTNSCVAVME GGEPVVIANP EGNRTTPSVV AFKNGEKIVG EAAKRQAITN
     PDNTVISIKR HMGTSHKETL EGNEYTPQQI SAMILQKLKS DAEAYLGESV TQAVITVPAY
     FNDSQRQATK DAGKIAGLEV LRIVNEPTAA ALAYGMEKSE DQTVLVFDLG GGTFDVSILE
     LSEGFFEVKA TSGDNKLGGD DFDQVVMDYL VSEFKKEHGI DLSKDRMAQQ RLKDAAEKAK
     KDLSGVLTTT ISLPFITADA TGPKHLEMNL TRAKFEELSS NLVERTMGPT RQALNDAGLT
     PNEIDKVILV GGSTRIPAVQ EAIKKFTGKE PHKGVNPDEV VALGAAVQAG VLTGDVKDVV
     LLDVTPLSLG IETLGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPGVEIHV LQGERQMAAD
     NKTLGRFNLN DIPPAPRGVP QIEVSFDIDA NGIVNVRAKD LGTGKEQRIT ITASSGLSDE
     EIDRMVKEAE LNAEADKQRK EQVEIRNEAD QLVFTTEKTL KEVEGKVDQA EIDRANAAKD
     KVKKALEGGS IDEIKSAKDE LSEIVQQISV KLYEQAAQAA GAAQGGAEGS AEPKKDNVVD
     ADYEVVDDKK