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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hyaENot known. Could form, along with HyaD, a complex involved in the processing of the hydrogenase 1 structural operon (132 aa)    
Predicted Functional Partners:
hyaD
Protease involved in the C-terminal processing of HyaB, the large subunit of hydrogenase 1
 
 
 0.998
hyaF
Not known. Could enhance the incorporation of nickel to the hydrogenase
 
  
 0.997
hyaC
Probable b-type cytochrome
 
  
 0.996
hyaA
This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth
 
 
 0.988
hyaB
This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth
 
 
 0.974
hybE
Hydrogenase-2 operon protein HybE; Member of hyb operon
  
   
 0.901
dsbE
Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD
   
 
 0.892
cbdB
A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
  
  
 0.786
cbdA
A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested . Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
  
  
 0.764
torS
Member of the two-component regulatory system TorS/TorR involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO). Detects the presence of TMAO in the medium and, in response, activates TorR via a four-step phosphorelay. When TMAO is removed, TorS can dephosphorylate TorR, probably by a reverse phosphorelay involving His- 860 and Asp-733
 
    0.746
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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