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
SEH92979.1Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. (619 aa)    
Predicted Functional Partners:
SEH92993.1
Protein of unknown function.
 
     0.951
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
  
 0.934
dnaJ
Molecular chaperone DnaJ; 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. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
  
 0.924
grpE
Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
 
 0.916
SEI10888.1
DnaJ domain-containing protein.
 
 0.880
SEI28594.1
Molecular chaperone DnaJ.
  
 0.880
SEH92733.1
DnaJ domain-containing protein.
  
 0.864
hscB
Molecular chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.
  
 
 0.811
SEH92966.1
Molecular chaperone DnaK (HSP70).
 
    
0.793
SEI22095.1
Ankyrin repeat.
   
 0.784
Your Current Organism:
Paraburkholderia hospita
NCBI taxonomy Id: 169430
Other names: Burkholderia hospita, Burkholderia hospita Goris et al. 2003, Burkholderia sp. LMG 20598, CCUG 43658, CCUG 43661, CIP 107793, DSM 17164, LMG 20598, LMG:20598, P. hospita, Paraburkholderia hospita (Goris et al. 2003) Sawana et al. 2015, strain Goris R-8366, strain R-8366
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