Types | DnaRegion
|
Roles | CDS
Coding
|
Sequences | BBa_K259000_sequence (Version 1)
|
Description
fhuA is an outer membrane (OM) protein that is found in the gram negative bacterium, E.coli. It is involved in the active-transport (energy-dependent uptake) of ferrichrome-iron from the extracellular environment. However fhuA is only able to bind ferrichrome-iron (i.e. ferrichrome iron is a ligand of fhuA protein). For the uptake to be completed fhuA needs to form a complex with another protein, tonB that carries out the energy-dependent uptake by using ATP as substrate to undergo the relevant conformational changes.
This biobrick ONLY encodes for fhuA.
fhuA is a beta-barell protein (22 anti-parallel beta-strands) and is composed of 747 aminoacids. This receptor protein may be used as an attachment point by some colicins.
References:
Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenusch J.P. and Moras D. (1998),Transmembrane signalling across the Ligand-Gated FhuAReceptor: Crystal structures of Free and Ferrichrome-Bound States reveal allosteric changes. Cell 95,771-778.
Uniprot access number: P06971
Ecogene: http://ecogene.org/geneInfo.php?eg_id=EG10302
Notes
The coding sequence (CDS) was already in compliance with assembly standard 10 (RFC10).
Source
fhuA is part of the chromosomal genome of E.coli. In particular it can be found at 3.61min and follows the clockwise direction.