STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dnaKMolecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. (643 aa)    
Predicted Functional Partners:
EH30_05980
Molecular chaperone GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
EH30_06005
Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, dnaK-independent fashion; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
groEL
Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...]
 
 0.999
EH30_15325
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.998
EH30_02775
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.990
EH30_10625
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.990
EH30_15855
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.990
EH30_08000
50S ribosomal protein L16; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.985
clpA
Clp protease ClpX; ATPase and specificity subunit of the ClpA-ClpP ATP dependent serine protease; directs protease to specific substrates; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.982
EH30_01505
ATPase AAA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.979
Your Current Organism:
Erythrobacter sp. JL475
NCBI taxonomy Id: 383381
Other names: E. sp. JL475
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.