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
AEB86537.1KEGG: dia:Dtpsy_3098 anti-sigma-28 factor, FlgM; TIGRFAM: Anti-sigma-28 factor, FlgM; PFAM: Anti-sigma-28 factor, FlgM. (107 aa)    
Predicted Functional Partners:
fliA
RNA polymerase, sigma 28 subunit, FliA/WhiG; 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.
  
 0.996
AEB86521.1
KEGG: dia:Dtpsy_3084 flagellar protein FliS; TIGRFAM: Flagellar protein FliS; PFAM: Flagellar protein FliS.
  
 
 0.972
AEB86538.1
Flagella basal body P-ring formation 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.
  
  
 0.928
AEB86539.1
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
  
  
 0.904
AEB86542.1
Flagellar hook-basal body protein; KEGG: aav:Aave_4423 hypothetical protein; TIGRFAM: Fagellar hook-basal body protein, FlgE/F/G; PFAM: Flagellar basal body FlaE; Domain of unknown function DUF1078, C-terminal; Flagellar basal body rod protein, N-terminal.
  
 
 0.903
AEB86540.1
KEGG: dia:Dtpsy_3101 flagellar basal-body rod protein FlgC; TIGRFAM: Flagellar basal-body rod protein FlgC; PFAM: Domain of unknown function DUF1078, C-terminal; Flagellar basal body rod protein, N-terminal; Belongs to the flagella basal body rod proteins family.
  
  
 0.902
AEB86541.1
Flagellar hook capping protein; Required for flagellar hook formation. May act as a scaffolding protein.
  
  
 0.900
AEB86522.1
Flagellar hook-associated 2 domain-containing 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.
  
  
 0.886
AEB86544.1
KEGG: dia:Dtpsy_3105 flagellar basal-body rod protein FlgG; TIGRFAM: Flagellar basal-body rod FlgG; Fagellar hook-basal body protein, FlgE/F/G; PFAM: Domain of unknown function DUF1078, C-terminal; Flagellar basal body rod protein, N-terminal; Belongs to the flagella basal body rod proteins family.
  
  
 0.886
AEB86512.1
Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
  
  
 0.882
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.