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bfd protein (Escherichia coli K12 MG1655) - STRING interaction network
"bfd" - Bacterioferritin-associated ferredoxin in Escherichia coli K12 MG1655
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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bfdBacterioferritin-associated ferredoxin; Seems to associate with BFR; could be a general redox and/or regulatory component participating in the iron storage mobilization functions of BFR. Could participate in the release or the delivery of iron from/to bacterioferritin (or other iron complexes) (64 aa)    
Predicted Functional Partners:
bfr
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule (158 aa)
 
 
 
  0.920
tonB
Protein TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy- dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to sp [...] (239 aa)
   
   
  0.817
fhuF
Ferric iron reductase protein FhuF; Involved in the reduction of ferric iron in cytoplasmic ferrioxamine B (262 aa)
   
   
  0.776
exbD
Biopolymer transport protein ExbD; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates (141 aa)
     
   
  0.755
entF
Enterobactin synthase component F; Activates the carboxylate group of L-serine via ATP- dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3- dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE) (1293 aa)
     
   
  0.665
entD
Enterobactin synthase component D; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4’- phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-form [...] (206 aa)
     
   
  0.581
ydeR
Putative fimbrial-like protein (167 aa)
           
  0.545
fecI
Probable RNA polymerase sigma factor FecI; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor regulates the fec genes for iron dicitrate transport (Probable) (173 aa)
     
   
  0.531
exbB
Biopolymer transport protein ExbB; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (244 aa)
     
   
  0.521
entE
Enterobactin synthase component E; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntE proccesses via a two-step adenylation- ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3- dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exc [...] (536 aa)
     
        0.514
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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