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
ANW23558.1Cobyrinic acid a,c-diamide synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (295 aa)    
Predicted Functional Partners:
flhF
Flagellar biosynthesis protein FlhF; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
fliA
RNA polymerase sigma factor FliA; 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.
 
  
 0.954
flhA
Flagellar biosynthesis protein FlhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
 
  
 0.917
ANW23598.1
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.
 
  
 0.900
ANW23604.1
Flagellar motor switch protein FliG; FliG 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.
 
  
 0.888
ANW25055.1
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.
 
  
 0.822
ANW23556.1
Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.815
fliG
Flagellar motor switch protein FliG; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.803
ANW24517.1
Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
  
 0.798
cheB
Chemotaxis response regulator protein-glutamate methylesterase; 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.
 
  
 0.783
Your Current Organism:
Vibrio coralliilyticus
NCBI taxonomy Id: 190893
Other names: ATCC BAA-450, CAIM 616, LMG 20984, LMG:20984, V. coralliilyticus, Vibrio coralliilyticus Ben-Haim et al. 2003, Vibrio corallilyticus, Vibrio coralyticus, Vibrio sp. LMG 10953, strain YB1
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