DNAK_CORJK
ID DNAK_CORJK Reviewed; 620 AA.
AC Q4JXX6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=jk0179;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36331.1; -; Genomic_DNA.
DR RefSeq; WP_005297124.1; NC_007164.1.
DR AlphaFoldDB; Q4JXX6; -.
DR SMR; Q4JXX6; -.
DR STRING; 306537.jk0179; -.
DR EnsemblBacteria; CAI36331; CAI36331; jk0179.
DR KEGG; cjk:jk0179; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000545; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..620
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225954"
FT REGION 492..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
FT /note="Basic and acidic residues"
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 620 AA; 66683 MW; 9674BD49A7981561 CRC64;
MGRAVGIDLG TTNSVVSVLE GGEAKVIANS EGSRTTPSIV AFAKNGEVLV GQSAKNQAVA
NVDRTIRSVK RHMGTDWKVS IDDKEYTAPE ISARTLQKLK RDAESYLGED VTDAVITVPA
YFNDAQRQAT KDAGQIAGLN VLRIVNEPTA AALAYGLEKG DKEQTILVFD LGGGTFDVSL
LEIGDGVVEV RATAGDNELG GDDWDQRIVD WLADKFKASH GVDLTKDKMA LQRLREAAEK
AKIELSSSQQ ASINLPYITV DEDRNPLFLD ETLTRTEFQK ITQDLLDRTK TPFQAVLKDA
EISVDEIDHV VLVGGSTRMV AVSELVTELT NGKEPNKGVN PDEVVAVGAA LQAGVLRGEV
KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTAEDSQPSV QIQVFQGERE
MAAHNKLLGS FELAGIAPAP RGVPQIEVTF DIDANGIVSV SAKDKATGKE NTIKIQDGSG
LSQEEIDRMV KDAETHAEED KKRREEQEVR NSAESMAYQT RKFVEDNKDK VSEDTQNKVE
EAAKAVDEAL KGDDIEAIKD AVEKLNAESQ EMGKAIYEAE AAAGAEGAGA DAAGSAANDD
PNVVDAEVVD EDTSAEDDKK