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.
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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
EEX37405.1Alkaline serine protease. (422 aa)    
Predicted Functional Partners:
EEX36157.1
Regulatory P domain of the subtilisin-like proprotein convertase.
  
  
0.847
EEX37984.1
MSHA biogenesis protein MshQ.
 
 0.832
EEX35830.1
Chromosome segregation ATPase.
  
 0.792
EEX37315.1
Microbial collagenase secreted.
 
 
 0.786
EEX35834.1
Hypothetical protein.
   
 0.785
EEX35750.1
Endonuclease I.
 
  
 0.719
dinB
DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
   
 
 0.600
EEX37519.1
Cell division protein FtsK.
  
 
 0.539
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.
    
 
 0.524
mrdB
Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily.
   
   0.513
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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