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
AQR95211.1PilZ domain protein. (224 aa)    
Predicted Functional Partners:
fliS
Flagellar protein FliS.
  
  
 0.709
fliM
Flagellar motor switch protein FliM.
  
 
 0.661
grsB
Gramicidin S synthase 2.
   
   0.648
flgK
Flagellar hook-associated protein 1; Belongs to the flagella basal body rod proteins family.
  
  
 0.643
fliN
Flagellar motor switch protein FliN.
  
  
 0.622
cheV
Chemotaxis protein CheV.
  
  
 0.620
AQR95959.1
Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
  
  
 0.619
fliD
Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
  
  
 0.619
AQR97029.1
Anti-sigma-28 factor, FlgM.
  
  
 0.615
motB_1
Motility protein B.
  
 
 0.608
Your Current Organism:
Clostridium saccharoperbutylacetonicum
NCBI taxonomy Id: 36745
Other names: ATCC 27021, C. saccharoperbutylacetonicum, Clostridium saccharoperbutylacetonicum Keis et al. 2001, DSM 14923, NCIMB 12606, strain N1-4 (HMT)
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