Disease relevance of enterobactin

• Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB [1].
• Ferric enterochelin transport in Yersinia enterocolitica: molecular and evolutionary aspects [2].
• The evidence suggests that tonB- strains lack an outer membrane component necessary both for the uptake of ferric-enterochelin and for the adsorption of phage phi80 [3].
• According to sequence alignment data and the coherent structure of the Yersinia fep-fes gene cluster, we suggest early genetic divergence of ferrienterochelin uptake determinants among species of the family Enterobacteriaceae [2].

High impact information on enterobactin

• We have determined the nucleotide sequence of the Escherichia coli fepA gene, which codes for the outer membrane receptor for ferrienterochelin and colicins B and D. The predicted FepA polypeptide has a molecular weight of 79,908 and consists of 723 amino acids [1].
• Some individuals had antibodies reacting very strongly with the iron-regulated outer membrane proteins, including the ferric-enterochelin receptor protein (Mr, 81,000), as well as with ompA [4].
• The compound removes iron from complexes with the host iron-binding proteins transferrin and lactoferrin, and the resulting ferric enterochelin is assimilated by the bacterial cell [5].
• Yersinia enterocolitica is well equipped for siderophore piracy, encompassing the utilization of siderophores such as ferrioxamine, ferrichrome, and ferrienterochelin [2].
• The deduced amino acid sequence of the amino-terminal portion of IrgA is homologous to the ferrienterochelin receptor of Escherichia coli (FepA), suggesting that IrgA may be the iron-vibriobactin outer membrane receptor [6].

Chemical compound and disease context of enterobactin

• The Escherichia coli gene for the ferrienterochelin uptake and colicins B and D receptor protein is located at approximately 13 min, adjacent to or among genes for enterochelin biosynthetic enzymes [7].

Anatomical context of enterobactin

• Spheroplasts of the former class transported ferric enterochelin, and those of the latter did not [8].

Associations of enterobactin with other chemical compounds

• The hydrolase described previously (Bryce, G.F. and Brot, N. (1972) Biochemistry 11, 1708-1715) as being able to break down enterochelin but not its iron complex, ferric-enterochelin, appears to be identical with the B component of enterochelin esterase [9].

Gene context of enterobactin

• This implies that an element of the inner membrane is affected. fep mutants were also unable to transport ferric enterochelin, and fell into two classes, fepA and fepB [8].
• Complementation tests with lambda hybrid phage were employed to distinguish the defective gene, which we term fepB, from fepA, the structural gene for the outer membrane ferrienterochelin receptor protein [10].
• On the other hand, the tonB mutant was unable to transport ferric enterochelin in either whole cells or spheroplasts [8].
• Effect of osmotic shock and shearing forces on ferric enterochelin transport in Escherichia coli K12 [11].
• The fes mutation in Escherichia coli K12, which inactivates enterochelin esterase, allows the cell to accumulate ferric enterochelin [11].

References