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.
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
bisCSimilar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (777 aa)    
Predicted Functional Partners:
bioB
Biotin synthetase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
     
  0.900
birA
biotin-[acetylCoA carboxylase] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
   
 
  0.900
msrP
Putative nitrate reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...]
      
 0.898
pbpC
Transglycosylase of penicillin-binding protein 1c; Similar to E. coli putative peptidoglycan enzyme (AAC75572.1); Blastp hit to AAC75572.1 (770 aa), 82% identity in aa 7 - 767.
      
 0.855
torD
Cytoplasmic chaperone which interacts with TorA; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor; Belongs to the TorD/DmsD family. TorD subfamily.
  
 
 0.834
yeaA
Hypothetical protein; Putative domain frequently associated with peptide methionine sulfoxide reductase; similar to E. coli orf, hypothetical protein (AAC74848.1); Blastp hit to AAC74848.1 (137 aa), 85% identity in aa 1 - 137.
      
 0.751
torC
Trimethylamine N-oxide reductase; Cytochrome c-type subunit; also has activity as negativer regulator of tor operon; similar to E. coli trimethylamine N-oxide reductase, cytochrome c-type subunit (AAC74081.1); Blastp hit to AAC74081.1 (390 aa), 90% identity in aa 1 - 388; Belongs to the TorC/TorY family.
 
 
 0.723
phsB
Hydrogen sulfide production iron-sulfur subunit; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsB subunit transfers electrons between PhsC and PhsA.
    
 
 0.706
msrA
Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
      
 0.685
msrQ
Putative inner membrane protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...]
      
 0.673
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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