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
azo2742Putative negative regulator of flagellin synthesis FlgM; Region start changed from 3024385 to 3024358 (27 bases). (98 aa)    
Predicted Functional Partners:
fliA
RNA polymerase sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes; Belongs to the sigma-70 factor family. FliA subfamily.
 
 0.999
flgN
Putative chaperon of flagella synthesis. FlgN is an export chaperon of FlgM and FlgK involved in flagellar synthesis. no signal peptide no TMHs; Family membership.
 
  
 0.992
fliS
Flagellar protein fliS. The function of this protein in flagellar biosynthesis is unknown, but appears to be regulatory. Might be a chaperon for Flic. InterPro: Flagellar protein FliS fliS: flagellar protein FliS Pfam: Flagellar protein FliS no signal peptide no TMHs; Family membership.
 
 
 0.990
flgA
Flagella basal body P-ring formation protein flgA precursor. 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 chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.976
fliL
Putative flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
  
 0.945
flgB
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
  
 0.945
flgK
Flagellar hook-filament junction protein 1 (HAP1). no signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.944
flgD
Probable basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein.
 
  
 0.941
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.
  
  
 0.931
fliD
Flagellar hook-associated 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.
 
  
 0.924
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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