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
trxBSimilar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. (322 aa)    
Predicted Functional Partners:
trxA
Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family.
 
 0.999
trxC
Similar to E. coli putative thioredoxin-like protein (AAC75635.1); Blastp hit to AAC75635.1 (139 aa), 94% identity in aa 1 - 139; Belongs to the thioredoxin family.
 
 0.996
ahpC
Alkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
  
 
 0.983
selD
Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP.
   
 
 0.922
sufS
Selenocysteine lyase; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
 
 
 0.921
STM1498
Similar to E. coli putative oxidoreductase, major subunit (AAC74660.1); Blastp hit to AAC74660.1 (808 aa), 91% identity in aa 2 - 807; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
     
 0.901
STM1499
Putative dimethyl sulphoxide reductase, chain A1; Similar to E. coli putative oxidoreductase, major subunit (AAC74659.1); Blastp hit to AAC74659.1 (808 aa), 86% identity in aa 1 - 808; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
     
 0.901
STM0402
Similar to E. coli alkyl hydroperoxide reductase, C22 subunit; detoxification of hydroperoxides (AAC73706.1); Blastp hit to AAC73706.1 (187 aa), 36% identity in aa 1 - 186.
  
 
 0.868
katE
Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.
   
 
 0.806
dsbC
Protein disulfide isomerase II; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase.
  
  
 0.805
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.