STRINGSTRING
fliF fliF flgB flgB flgC flgC fliE fliE flgG flgG flgA flgA flgI flgI flgH flgH AIL98493.1 AIL98493.1 flgE flgE flgK flgK flgD flgD
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:
fliFFlagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (557 aa)
flgBFlagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (126 aa)
flgCWith FlgF and B makes up the proximal portion of the flagellar basal body rod; Bradyrhizobium have one thick flagellum and several thin flagella; the protein in this cluster is associated with the thin flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (139 aa)
fliEFlagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. (111 aa)
flgGFlagellar basal-body rod protein FlgG; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. (262 aa)
flgAFlagellar basal body P-ring biosynthesis protein FlgA; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. (169 aa)
flgIFlagellar P-ring protein FlgI; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (371 aa)
flgHFlagellar L-ring protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (236 aa)
AIL98493.1Flagellar basal body protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (163 aa)
flgEFlagellar hook protein FlgE; Derived by automated computational analysis using gene prediction method: Protein Homology. (406 aa)
flgKWith FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. (472 aa)
flgDActs as a scaffold for the assembly of hook proteins onto the flagellar basal body rod; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of some flagellar genes; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thin flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (138 aa)
Your Current Organism:
Sinorhizobium meliloti
NCBI taxonomy Id: 382
Other names: ATCC 9930, CCUG 27879, CFBP 5561, DSM 30135, Ensifer meliloti, Ensifer sp. AC50a, Ensifer sp. AC50e, HAMBI 2148, IAM 12611, ICMP 12623, IFO 14782, JCM 20682, LMG 6133, LMG:6133, NBRC 14782, NCAIM B.01520, NRRL L-45, NZP 4027, Rhizobium meliloti, Rhizobium meliloti (megaplasmid pRME41B SYM), Rhizobium meliloti (plasmid pRmeGR4b), Rhizobium meliloti plasmid pRmeGR4b, Rhizobium sp. AC50e, S. meliloti
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