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
EEX36157.1Regulatory P domain of the subtilisin-like proprotein convertase. (556 aa)    
Predicted Functional Partners:
EEX37984.1
MSHA biogenesis protein MshQ.
  
 0.986
EEX35830.1
Chromosome segregation ATPase.
  
 0.986
EEX35834.1
Hypothetical protein.
   
 0.968
EEX37315.1
Microbial collagenase secreted.
 
 
 0.942
EEX35750.1
Endonuclease I.
 
  
  0.800
EEX36901.1
Secreted trypsin-like serine protease; COG5640.
  
 
 0.773
EEX35989.1
Secreted trypsin-like serine protease; COG5640.
 
 
 0.773
EEX36022.1
Secreted trypsin-like serine protease.
  
 
 0.773
EEX37937.1
Endonuclease I precursor.
    
  0.761
secY
Preprotein translocase SecY 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.
    
 
 0.682
Your Current Organism:
Vibrio metschnikovii
NCBI taxonomy Id: 675813
Other names: V. metschnikovii CIP 69.14, Vibrio metschnikovii CIP 69.14, Vibrio metschnikovii str. CIP 69.14, Vibrio metschnikovii strain CIP 69.14
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