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
HA50_11575Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (435 aa)    
Predicted Functional Partners:
HA50_11585
Flagellar export chaperone FliS; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
flgL
With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.975
HA50_07615
Flagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
 
 0.974
HA50_11580
Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
 
 
 0.971
flgK
Flagellar hook-associated protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.969
HA50_11640
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.
 
  
 0.964
HA50_07620
Flagellar basal body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family.
 
  
 0.963
fliI
Flagellum-specific ATP synthase FliI; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.962
HA50_11670
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.
 
  
 0.958
HA50_28980
Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
 
 
 0.957
Your Current Organism:
Pantoea cypripedii
NCBI taxonomy Id: 55209
Other names: ATCC 29267, Bacillus cypripedii, CFBP 3613, CIP 105195, DSM 3873, Erwinia carotovora var. cypripedii, Erwinia cypripedii, Erwinia cyrpipedii, LMG 2655, LMG 2657, LMG:2655, LMG:2657, NCPPB 3004, P. cypripedii, Pectobacterium cypripedii
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