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
fxsAInner membrane protein; Protein involved in (DEPRECATED) molecular function unknown and (DEPRECATED) biological process unknown. (175 aa)    
Predicted Functional Partners:
ybbN
Predicted thioredoxin domain-containing protein; Protein involved in (DEPRECATED) molecular function unknown and (DEPRECATED) biological process unknown.
   
    0.616
hslV
Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
    0.616
ADM98267.1
Twin-arginine translocation signal domain protein; Protein involved in (DEPRECATED) molecular function unknown and (DEPRECATED) biological process unknown.
  
    0.605
groS
Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
  
 0.562
hslU
Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
    0.499
ibpB
Heat shock chaperone; Protein involved in response to temperature stimulus; Belongs to the small heat shock protein (HSP20) family.
  
    0.489
htpX
Protein involved in metalloendopeptidase activity, zinc ion binding, response to temperature stimulus and proteolysis; Belongs to the peptidase M48B family.
   
  
 0.462
groL
Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
       0.441
Dda3937_02464
Small heat shock protein; Belongs to the small heat shock protein (HSP20) family.
   
    0.404
ibpA
Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
   
    0.404
Your Current Organism:
Dickeya dadantii
NCBI taxonomy Id: 198628
Other names: D. dadantii 3937, Dickeya dadantii 3937, Dickeya dadantii str. 3937, Dickeya dadantii strain 3937, Erwinia chrysanthemi str. 3937, Pectobacterium chrysanthemi str. 3937
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