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
KYG_18219DoxX family protein. (137 aa)    
Predicted Functional Partners:
KYG_18214
COG1741 Pirin-related protein; Belongs to the pirin family.
  
  
 0.674
KYG_18224
Flavodoxin/nitric oxide synthase; COG0655 Multimeric flavodoxin WrbA.
  
    0.610
KYG_22855
Hypothetical protein.
  
  
 0.572
KYG_22860
COG3220 Uncharacterized protein conserved in bacteria; Belongs to the UPF0276 family.
  
  
 0.571
KYG_18229
COG1741 Pirin-related protein; Belongs to the pirin family.
  
  
 0.494
KYG_18209
COG0583 Transcriptional regulator; Belongs to the LysR transcriptional regulatory family.
       0.481
KYG_17909
COG2010 Cytochrome c, mono- and diheme variants.
    
  0.414
secY
Preprotein translocase subunit SecY; 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.
   
 
 0.404
Your Current Organism:
Nocardioides sp. SLBN35
NCBI taxonomy Id: 512030
Other names: Acidovorax sp. NO1, N. sp. SLBN-35, Nocardioides sp. SLBN-35
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.