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
fliMFlagellar 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. (334 aa)    
Predicted Functional Partners:
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.
 
 0.999
fliG
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.
 
 0.998
AOP79245.1
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.
 
 0.997
AOP79238.1
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.
 
 0.996
fliL
Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
 
 0.992
AOP78626.1
Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
 0.991
AOP78635.1
Flagellar biosynthetic protein FliO; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.991
flgJ-2
Flagellar rod assembly protein/muramidase FlgJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.991
AOP78638.1
Flagellar biosynthetic protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family.
 
  
 0.987
fliQ
Flagellar export apparatus protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family.
 
  
 0.986
Your Current Organism:
Enterobacter hormaechei steigerwaltii
NCBI taxonomy Id: 299766
Other names: CIP 108489, DSM 16691, E. hormaechei subsp. steigerwaltii, Enterobacter hormaechei subsp. steigerwaltii, Enterobacter hormaechei subsp. steigerwaltii Hoffmann et al. 2016, Enterobacter sp. GN02457, accession AJ543908, accession AJ853890, strain EN-562
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