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
AJF87669.1Siderophore ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily. (333 aa)    
Predicted Functional Partners:
fecE
Iron-dicitrate transporter ATP-binding subunit; Part of the FecBCDE citrate-dependent iron (III) transport system; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
AJF84087.1
Iron citrate ABC transporter substrate-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.970
fecD
Iron-dicitrate transporter subunit FecD; Ferric citrate binds FecA and is transported across the outer membrane while transmits a signal across the cytoplasmic membrane protein FecR. FecR transmits a signal across the membrane and activates the cytoplasmic FecI that directs the RNA polymerase to express the fecABCDE operon (which encodes the ferric citrate outer membrane receptor and the ferric citrate ABC transporter), as well as fecIR. FecD is one of two (along with FecC) integral membrane protein components of the iron dicitrate ABC transporter; Derived by automated computational an [...]
 
 
 
0.969
fecE-2
Iron-dicitrate transporter ATP-binding subunit; Part of the FecBCDE citrate-dependent iron (III) transport system; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.922
AJF86365.1
ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.919
AJF86386.1
Iron ABC transporter ATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.914
AJF84345.1
Siderophore ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
  
  
 
0.906
AJF86388.1
Iron ABC transporter substrate-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  0.844
fecD-2
Iron-dicitrate transporter subunit FecD; Ferric citrate binds FecA and is transported across the outer membrane while transmits a signal across the cytoplasmic membrane protein FecR. FecR transmits a signal across the membrane and activates the cytoplasmic FecI that directs the RNA polymerase to express the fecABCDE operon (which encodes the ferric citrate outer membrane receptor and the ferric citrate ABC transporter), as well as fecIR. FecD is one of two (along with FecC) integral membrane protein components of the iron dicitrate ABC transporter; Derived by automated computational an [...]
 
 
 
0.843
AJF84166.1
Iron siderophore-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.656
Your Current Organism:
Bacillus atrophaeus
NCBI taxonomy Id: 1452
Other names: ATCC 49337, B. atrophaeus, Bacillus atriphaeus, Bacillus sp. S2 BC-2, Bacillus subtilis DSM 2277, Bacillus subtilis DSM 675, CCUG 28524, CIP 107159, DSM 7264, IFO 15539, JCM 9070, LMG 16797, LMG:16797, NBRC 15539, NRRL NRS-213
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