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
motBFlagellar motor protein MotB; With MotA forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; Vibrio parahaemolyticus protein is associated with the polar flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (307 aa)    
Predicted Functional Partners:
KPM83652.1
Flagellar motor protein PomA; Homologous to MotA in E. coli and Salmonella. With PomB forms the ion channels that couple flagellar rotation to sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
motC
Flagellar motor protein; Homologous to MotA; this protein with a related protein (a MotB homolog) forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; either MotAB or MotCD is sufficient for swimming, but both are necessary for swarming motility; these organisms have both MotA and MotC; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
KPM83355.1
Chemotaxis protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.937
KPM83411.1
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.
 
  
 0.880
KPM83375.1
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.
 
 
 0.876
KPM82345.1
Outer membrane lipid asymmetry maintenance protein MlaD; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.875
KPM85315.1
Flagellar basal body-associated protein FliL-like protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
 
 0.871
KPM83403.1
Flagellar biosynthesis protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.861
KPM84932.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.859
fliL
Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
 
 
 0.850
Your Current Organism:
Pseudoalteromonas lipolytica
NCBI taxonomy Id: 570156
Other names: CGMCC 1.8499, JCM 15903, P. lipolytica, Pseudoalteromonas lipolytica Xu et al. 2010, Pseudoalteromonas sp. ASS5B, Pseudoalteromonas sp. ASW16, strain LMEB 39
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