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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
KKF34864.1Flagellar basal body P-ring biosynthesis protein FlgA; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. (222 aa)    
Predicted Functional Partners:
flgJ
Flagellar rod assembly protein FlgJ; Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.998
KKF34863.1
Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
  
 0.991
flgD
Flagellar basal body rod modification protein; Required for flagellar hook formation. May act as a scaffolding protein.
 
  
 0.989
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.
 
  
 0.987
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.
 
  
 0.982
flgK
With 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.
 
  
 0.973
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.
 
  
 0.971
flgI
Flagellar basal body P-ring biosynthesis protein FlgA; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.971
flgF
Flagellar basal body rod protein FlgF; FlgF, with FlgB and C, makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.971
flgG
Makes up the distal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.969
Your Current Organism:
Erwinia tracheiphila
NCBI taxonomy Id: 65700
Other names: ATCC 33245, Bacillus tracheiphilus, Bacterium tracheiphilus, CFBP 2355, CIP 105205, DSM 21139, E. tracheiphila, Erwinia amylovora var. tracheiphila, ICMP 5845, LMG 2707, LMG 2906, LMG:2707, LMG:2906, NCPPB 2452
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