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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
flhAFlagellar biosynthesis protein; 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. (694 aa)    
Predicted Functional Partners:
flhB
Flagellar biosynthetic protein; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family.
 
 0.999
fliF
Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
  
 0.990
fliR
Flagellar biosynthetic protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family.
 
  
 0.988
fliM
Flagellar motor switch protein; 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.
 
  
 0.988
fliP
Flagellar biosynthetic protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family.
 
  
 0.987
fliG
Flagellar motor switch protein; 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.
 
  
 0.987
fliQ
Flagellar biosynthetic protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family.
 
  
 0.976
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.
 
  
 0.970
fliH
Similar to Salmonella typhimurium flagellar assembly protein FliH or Fla BIII or Fla AII.3 or stm1971 SWALL:FLIH_SALTY (SWALL:P15934) (235 aa) fasta scores: E(): 1.6e-43, 58.36% id in 245 aa.
 
 
 0.969
fliI
Similar to Salmonella typhimurium flagellum-specific ATP synthase FliI or Fla AIII or FlaC or stm1972 SWALL:FLII_SALTY (SWALL:P26465) (456 aa) fasta scores: E(): 1.5e-139, 85.24% id in 454 aa.
 
 
 0.967
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.