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
flgKWith FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. (547 aa)    
Predicted Functional Partners:
flgL
Flagellar biosynthesis protein FlgL; With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.998
flgE
Flagellar biosynthesis protein FlgE; The hook connects flagellar basal body to the flagellar filament; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.997
fliS
Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.993
fliD
Flagellar filament capping 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).
 
  
 0.993
flgH
Flagellar basal body L-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
 0.992
flgC
With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.991
flgB
Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity).
 
  
 0.989
flgG
Flagellar basal-body rod protein FlgG; Makes up the distal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.989
flgI
Flagellar biosynthesis protein FlgA; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.989
fliM
Flagellar motor switch protein FliM; FliM 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.
 
  
 0.986
Your Current Organism:
Proteus mirabilis
NCBI taxonomy Id: 584
Other names: ATCC 29906, CCUG 26767, CIP 103181, DSM 4479, LMG 3257, LMG:3257, NCTC 11938, P. mirabilis
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