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
fliN-2Flagellar motor switch protein; FliN is one of three proteins (FliG, FliN, FliM) that form 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. Belongs to the FliN/MopA/SpaO family. (117 aa)    
Predicted Functional Partners:
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.
 
 0.999
fliG
Flagellar motor switch protein FliG; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
fliF
Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
 
 0.998
fliH
Flagellar assembly protein H; Binds to and inhibits the function of flagella specific ATPase FliI; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.996
fliI
ATP synthase; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.992
flgC
Flagellar basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family.
 
 
 0.991
flgK
Flagellar basal body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family.
 
 
 0.989
flgG
Makes up the distal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagella; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.987
ispDF
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
   
   0.985
fliQ
Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family.
 
  
 0.985
Your Current Organism:
Afipia massiliensis
NCBI taxonomy Id: 211460
Other names: A. massiliensis, Afipia massiliensis La Scola et al. 2002, Afipia sp. LC387, CCUG 45153, CIP 107022, DSM 17498, strain 34633
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.