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
flaBFlagellin FlaB; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaB is not essential for flagellar synthesis and motility (By similarity). (376 aa)    
Predicted Functional Partners:
fliS
Flagellar protein FliS; Similar to GB:U12816 PID:1254205; identified by sequence similarity; putative.
 
 
 0.993
fliD
Flagellar hook-associated protein FliD; Required for the 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 (By similarity).
 
 
 0.965
VC_2130
Flagellum-specific ATP synthase FliI; Similar to PID:1071643 SP:P52612 GB:U00096 PID:1736607 PID:1788251; identified by sequence similarity; putative.
 
 
 0.942
fliG
Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
 
  
 0.938
VC_2125
Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
 
 
 0.937
flaG
Flagellin FlaG; Similar to PID:2271029; identified by sequence similarity; putative; To FlaG in other Vibrio species.
  
 
 0.928
VC_2195
Flagellar basal-body rod protein FlgG; Similar to GB:U00096 SP:P75939 PID:1787318; identified by sequence similarity; putative; Belongs to the flagella basal body rod proteins family.
 
 
 0.927
flhB
Flagellar biosynthetic protein FlhB; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family.
 
  
 0.923
VC_2191
Flagellar hook-associated protein FlgM; Similar to PID:2443633; identified by sequence similarity; putative.
 
  
 0.922
VC_2199
Flagellar basal-body rod protein FlgC; Similar to GB:U00096 SP:P75935 PID:1787314; identified by sequence similarity; putative; Belongs to the flagella basal body rod proteins family.
 
  
 0.917
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.