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
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Textmining
[Homology]
Score
flgFFlagellar basal-body rod protein flgF (Putative proximal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. (245 aa)    
Predicted Functional Partners:
flgI
Flagellar P-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
 
 0.998
flgH
Flagellar L-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
 
 0.998
flgD
Probable basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein.
 
 
 0.998
flgC
Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
 
 
 0.998
flgB
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
 
 0.998
flgG
Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
 
0.997
flgE
Flagellar hook protein flgE. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
 
 
0.997
fliF
Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
  
 
 0.994
fliM
Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE 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. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity.
  
 
 0.993
flgJ
Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.991
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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