ID   DNAK_CORGB              Reviewed;         618 AA.
AC   A4QHJ0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=cgR_2690;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF55706.1; -; Genomic_DNA.
DR   RefSeq; WP_003853569.1; NC_009342.1.
DR   AlphaFoldDB; A4QHJ0; -.
DR   SMR; A4QHJ0; -.
DR   EnsemblBacteria; BAF55706; BAF55706; cgR_2690.
DR   GeneID; 58309087; -.
DR   KEGG; cgt:cgR_2690; -.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; A4QHJ0; -.
DR   Proteomes; UP000006698; Chromosome.
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; 2.
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..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059547"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   618 AA;  66331 MW;  ABC26715F6139054 CRC64;
     MGRAVGIDLG TTNSVVSVLE GGEPVVIANA EGSRTTPSVV AFAKNGEVLV GQSAKNQAVT
     NVDRTIRSVK RHIGTDWSVA IDDKNYTSQE ISARTLMKLK RDAEAYLGED VTDAVITVPA
     YFEDSQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLEKG EQEQTILVFD LGGGTFDVSL
     LEIGDGVVEV RATSGDNELG GDDWDQRIVD WLVEKFQSSN GIDLTKDKMA LQRLREAAEK
     AKIELSSSQS ANINLPYITV DADKNPLFLD ETLSRAEFQR ITQDLLDRTK TPFNQVVKDA
     GVSVSEIDHV VLVGGSTRMP AVTELVKELT GGREPNKGVN PDEVVAVGAA LQAGVLRGEV
     KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTAEDNQPSV QIQVFQGERE
     IATANKLLGS FELGGIAPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTITIQDGSG
     LSQDEIDRMI KDAEAHADED KKRREEQEVR NNAESLVYQT RKFVEENSEK VSEDLKAKVE
     EAAKGVEEAL KGEDLEAIKA AVEKLNTESQ EMGKAIYEAD AAAGATQADA GAEGAADDNV
     VDAEVVEDDA ADNGEDKK