DNAK_COREF
ID DNAK_COREF Reviewed; 619 AA.
AC Q8FM78;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CE2629;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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; BA000035; BAC19439.1; -; Genomic_DNA.
DR RefSeq; WP_006769007.1; NZ_GG700685.1.
DR AlphaFoldDB; Q8FM78; -.
DR SMR; Q8FM78; -.
DR STRING; 196164.23494473; -.
DR PRIDE; Q8FM78; -.
DR EnsemblBacteria; BAC19439; BAC19439; BAC19439.
DR KEGG; cef:CE2629; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001409; 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..619
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078453"
FT REGION 582..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 619 AA; 66658 MW; 4CF9AD9BB84E0615 CRC64;
MGRAVGIDLG TTNSVVSVLE GGEPVVIANS EGSRTTPSVV AFAKNGEVLV GQSAKNQAVT
NVDRTIRSVK RHIGTDWSVA IDDKNYTAQE ISARILMKLK RDAEAYLGEE VTDAVITVPA
YFEDSQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLEKG EQEQTILVFD LGGGTFDVSL
LEIGDGVVEV RATSGDNELG GDDWDQRIVD WLVEKFQSSH GIDLTKDKMA LQRLREAAEK
AKIELSASQN ANINLPYITV DADKNPLFLD ENLSRAEFQR ITQDLLDRTK TPFNQVIKDA
GISVSEIDHV VLVGGSTRMP AVTDLVKELT GGREPNKGVN PDEVVAVGAA LQAGVLRGEV
KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTAEDNQPSV QIQVFQGERE
IASANKLLGS FELGGIAPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTITIQDGSG
LSQEEIDRMI KDAEAHAEED KKRREEQEIR NNAESLVYQT HKFVEENDGK ISEELKGKVE
EAAKGVEETL KGEDIDAIKT AVDKLNTESQ EMGRAIYEAE AAAGATQADA GAEGAADDNV
VDAEVVDEDV SEEKKDGDK