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
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[Homology]
Score
fliTFlagellar biosynthesis protein FliT; Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus. (121 aa)    
Predicted Functional Partners:
fliS
Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.982
fliD
Flagellar cap protein FliD; 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.
  
 
 0.977
flgN
Flagellar biosynthesis protein FlgN; Export chaperone for FlgK and FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.722
fliN
Flagellar motor switch protein FliN; 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.
   
  
 0.688
fliZ
Flagellar biosynthesis protein FliZ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.677
cheR
Chemotaxis protein CheR; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
   
  
 0.660
cheW
Chemotaxis protein CheW; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.654
flgM
Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.644
cheA
Chemotaxis protein CheA; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.625
cheB
Chemotaxis protein; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
   
  
 0.611
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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