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
fxsAExclusion suppressor FxsA; Derived by automated computational analysis using gene prediction method: Protein Homology. (166 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
    0.768
ybbN
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.765
groES
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
  
 0.653
hslU
ATP-dependent protease ATP-binding subunit HslU; 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.
   
    0.541
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
     
 0.536
cutA
Cation tolerance protein CutA; Involved in resistance toward heavy metals. Belongs to the CutA family.
     
 0.533
yjdC
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.471
maeB
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.468
htpX
Heat shock protein HtpX; Metalloprotease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family.
   
  
 0.455
hslT
Heat shock protein IbpA; 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.
   
    0.445
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.