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
Rmet_0996Peptidase S8 and S53, subtilisin, kexin, sedolisin precursor. (540 aa)    
Predicted Functional Partners:
Rmet_2594
Conserved hypothetical protein (secreted).
 
 
 0.557
Rmet_3467
Putative bifunctional P-450:NADPH-P450 reductase 2 (Includes: Cytochrome P450 102; NADPH--cytochrome P450 reductase).
  
 0.548
Rmet_0997
Conserved hypothetical protein.
       0.532
ctpF
Cation-transporting ATPase F.
   
 0.532
Rmet_0551
Putative hypothetical transmembrane protein.
  
 
 0.497
Rmet_2057
Hemagglutinin-related transmembrane protein.
  
 
 0.497
Rmet_1695
Conserved hypothetical protein.
  
 
 0.492
Rmet_0083
Conserved hypothetical protein.
  
 
 0.491
recN
Recombination and repair protein; May be involved in recombinational repair of damaged DNA.
       0.468
secY
Preprotein translocase membrane subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
    
 
 0.465
Your Current Organism:
Cupriavidus metallidurans
NCBI taxonomy Id: 266264
Other names: C. metallidurans CH34, Cupriavidus metallidurans CH34, Cupriavidus metallidurans str. CH34, Cupriavidus metallidurans strain CH34, Ralstonia metallidurans CH34, Wautersia metallidurans CH34
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.