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
LSS_09189Flagellar 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. (341 aa)    
Predicted Functional Partners:
LSS_02649
Endoflagellar motor switch protein; 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
LSS_09139
Endoflagellar motor switch protein; 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
LSS_15271
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
LSS_16806
Endoflagellar motor switch protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
flgB
Flagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
 
 0.996
LSS_02237
Flagellar hook protein FlgE; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.995
LSS_11640
Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
 
 0.995
LSS_11635
Endoflagellar motor switch protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 
 0.994
flgC
With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.993
fliE
Flagellar hook-basal body protein FliE; Forms a junction between the M-ring and FlgB during the flagella biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.993
Your Current Organism:
Leptospira santarosai
NCBI taxonomy Id: 758847
Other names: L. santarosai serovar Shermani str. LT 821, Leptospira santarosai serovar Shermani LT 821, Leptospira santarosai serovar Shermani str. ATCC 43286, Leptospira santarosai serovar Shermani str. LT 821, Leptospira santarosai serovar Shermani strain LT 821
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.