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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
fxsAProtein FxsA (suppressor of F exclusion of phage T7). (158 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
    0.823
ROD_05471
Thioredoxin-like protein.
   
    0.821
cutA
Divalent cation tolerance protein; Involved in resistance toward heavy metals. Belongs to the CutA family.
     
 0.615
htpX
Probable protease (heat shock protein); Belongs to the peptidase M48B family.
   
  
 0.611
hslU
ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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.
   
    0.605
ROD_31981
Putative transcriptional regulator.
     
 0.479
aspA
Aspartate ammonia-lyase.
       0.478
nnrD
Putative carbohydrate kinase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of [...]
      
 0.476
hslS
Small heat shock protein B; Associates with aggregated proteins, together with IbpA, 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.
  
    0.475
ROD_32081
Putative lipoprotein.
     
 0.454
Your Current Organism:
Citrobacter rodentium
NCBI taxonomy Id: 637910
Other names: C. rodentium ICC168, Citrobacter rodentium ICC168, Citrobacter rodentium str. ICC168, Citrobacter rodentium strain ICC168
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