ID   DNAK_CORGL              Reviewed;         618 AA.
AC   Q8NLY6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
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};
GN   OrderedLocusNames=Cgl2800, cg3100;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; BA000036; BAC00194.1; -; Genomic_DNA.
DR   EMBL; BX927156; CAF20821.1; -; Genomic_DNA.
DR   RefSeq; NP_601992.1; NC_003450.3.
DR   RefSeq; WP_011015390.1; NC_006958.1.
DR   AlphaFoldDB; Q8NLY6; -.
DR   SMR; Q8NLY6; -.
DR   STRING; 196627.cg3100; -.
DR   World-2DPAGE; 0001:Q8NLY6; -.
DR   KEGG; cgb:cg3100; -.
DR   KEGG; cgl:Cgl2800; -.
DR   PATRIC; fig|196627.13.peg.2732; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000582; 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   Reference proteome; Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078454"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   618 AA;  66287 MW;  5F71F1F1F5A2C456 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 ITQDLLARTK 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