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 27-MAR-2024, entry version 93.
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; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; 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 GeneID; 69623079; -.
DR KEGG; cgt:cgR_2690; -.
DR HOGENOM; CLU_005965_2_4_11; -.
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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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
//
