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
fliKSimilar to Salmonella typhimurium flagellar hook-length control protein FliK or FlaE or FlaR or stm1974 SWALL:FLIK_SALTY (SWALL:P26416) (405 aa) fasta scores: E(): 1.9e-22, 35.3% id in 405 aa. (432 aa)    
Predicted Functional Partners:
fliF
Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
  
 0.997
fliJ
Flagellar protein; Flagellar protein that affects chemotactic events. Belongs to the FliJ family.
 
  
 0.996
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.
 
  
 0.996
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.
 
  
 0.994
flgJ
Peptidoglycan hydrolase; Similar to Salmonella typhimurium peptidoglycan hydrolase FlgJ or FlaZ or Fla FX or stm1182 SWALL:FLGJ_SALTY (SWALL:P15931) (316 aa) fasta scores: E(): 8.9e-65, 61.49% id in 322 aa.
 
  
 0.993
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.
 
  
 0.991
fliO
Flagellar protein; Previously sequenced as Erwinia carotovora MopB protein mopB SWALL:MOPB_ERWCA (SWALL:P34199) (140 aa) fasta scores: E(): 2.5e-48, 95% id in 140 aa, and to Salmonella typhimurium, and Salmonella typhi flagellar protein flio flio or flbd or flap or stm1978 or sty2186 SWALL:FLIO_SALTY (SWALL:P54699) (125 aa) fasta scores: E(): 2.9e-14, 45% id in 120 aa.
 
  
 0.990
fliL
Flagellar protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
  
 0.989
flgD
Basal-body rod modification protein; Required for flagellar hook formation. May act as a scaffolding protein.
 
 
 0.988
flgH
Flagellar L-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.986
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
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