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
fxsAMembrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (153 aa)    
Predicted Functional Partners:
hslV
HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
    0.680
ybbN
Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.679
groES
Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
  
 0.528
ibpA
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.
   
    0.446
hslU
HslU--HslV peptidase ATPase subunit; 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.
   
    0.435
DSJ_03760
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.428
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
       0.418
cutA
Divalent-cation tolerance protein CutA; Involved in resistance toward heavy metals.
     
 0.416
Your Current Organism:
Pantoea stewartii
NCBI taxonomy Id: 660596
Other names: P. stewartii subsp. stewartii DC283, Pantoea stewartii subsp. stewartii DC283, Pantoea stewartii subsp. stewartii str. DC283, Pantoea stewartii subsp. stewartii strain DC283
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