Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Chaperone protein DnaK  

UniProtKB / Swiss-Prot ID :  DNAK_ECOLI

Gene Name (Synonyms) : 
dnaK, groP, grpF, seg b0014, JW0013  

Species :  Escherichia coli (strain K12). 

Subcellular Localization :  Cytoplasm. Cell inner membrane; Peripheral membrane protein. 

Protein Function :  Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock. 

Protein Sequence MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIK...
Predicted Secondary Structure CCEEEEEEECCCCEEEEEEECCEEEEEECCCCCCCCCEEEEECCCCCEEECCHHHCCCCCCHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
70N6-succinyllysine.LFAIKRLIG
HHHHHHHHC
37.41UniProtKB
Link-
109N6-acetyllysine.VKGQKMAPP
ECCCEECHH
45.78UniProtKB
Link-
199Phosphothreonine; by autocatalysis.LGGGTFDIS
ECCCEEEEE
22.78UniProtKB
Link-
245N6-acetyllysine; alternate.VEEFKKDQG
HHHHHHHHC
59.73UniProtKB
Link-
245N6-succinyllysine; alternate.VEEFKKDQG
HHHHHHHHC
59.73UniProtKB
Link-
246N6-succinyllysine.EEFKKDQGI
HHHHHHHCC
61.68UniProtKB
Link-
304N6-acetyllysine; alternate.VTRAKLESL
ECHHHHHHH
49.88UniProtKB
Link-
304N6-succinyllysine; alternate.VTRAKLESL
ECHHHHHHH
49.88UniProtKB
Link-
359N6-succinyllysine.EFFGKEPRK
HHHCCCCCC
60.43UniProtKB
Link-
421N6-acetyllysine.TIPTKHSQV
CCCCEEEEE
35.58UniProtKB
Link
502N6-succinyllysine.KITIKASSG
EEEEECCCC
33.30UniProtKB
Link
528N6-succinyllysine.EADRKFEEL
HHHHHHHHH
58.64UniProtKB
Link
556N6-acetyllysine.EAGDKLPAD
HHHHCCCHH
56.29UniProtKB
Link-
587N6-succinyllysine.AIEAKMQEL
HHHHHHHHH
28.46UniProtKB
Link-
635Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)FEEVKDKK
EEECCCCC
68.08PupDB
Link-
637Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)EVKDKK
ECCCCC
55.45PupDB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation is a highly abundant and evolutionarily conservedmodification in Escherichia coli.";
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,Grishin N.V., Zhao Y.;
Mol. Cell. Proteomics 8:215-225(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-245; LYS-304;LYS-421 AND LYS-556, AND MASS SPECTROMETRY.
N6-succinyllysine
ReferencePubMed
"Identification of lysine succinylation as a new post-translationalmodification.";
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
Nat. Chem. Biol. 7:58-63(2011).
Cited for: SUCCINYLATION AT LYS-70; LYS-245; LYS-246; LYS-304; LYS-359; LYS-502;LYS-528 AND LYS-587.
Phosphorylation
ReferencePubMed
"DnaK as a thermometer: threonine-199 is site of autophosphorylationand is critical for ATPase activity.";
McCarty J.S., Walker G.C.;
Proc. Natl. Acad. Sci. U.S.A. 88:9513-9517(1991).
Cited for: PHOSPHORYLATION AT THR-199.
"Inhibition of DnaK autophosphorylation by heat shock proteins andpolypeptide substrates.";
Panagiotidis C.A., Burkholder W.F., Gaitanaris G.A., Gragerov A.,Gottesman M.E., Silverstein S.J.;
J. Biol. Chem. 269:16643-16647(1994).
Cited for: PHOSPHORYLATION AT THR-199.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures