1 Child Features
| DB identifier | Type | Name |
|---|---|---|
| IPR010065 | Domain | Amino acid ABC transporter, permease protein, 3-TM domain |
| Type: | Domain | Name: | ABC transporter type 1, transmembrane domain MetI-like |
| Description: | ABC transporters are minimally constituted of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These regions can be found on the same protein (mostly in eukaryotes and bacterial exporters) or on two different ones (mostly bacterial importers) []. In importers, the TMD displays a distinctive signature, the EAA motif, a 20 amino acid conserved sequence located about 100 residues from the C terminus. The motif is hydrophilic and has been found to reside in a cytoplasmic loop located between the penultimate and the antepenultimate transmembrane segment in all proteins with a known topology []. It appears to play an important role in ensuring the correct assembly of the prokaryotic ABC transport complex [] and constituting an interaction site with the so-called helical domain of the ABC module [, ].This entry recognises ABC transmembrane domains where the TMD is on a separate protein, such as the D-methionine transport system permease protein MetI. The crystal structure of the high-affinity Escherichia coli MetNI methionine uptake transporter has been solved. Each MetI subunit is organised around a core of five transmembrane helices that correspond to a subset of the helices observed in the larger membrane-spanning subunits of the molybdate (ModBC) and maltose (MalFGK) ABC transporters, which contain six helices []. | Short Name: | MetI-like |
| DB identifier | Type | Name |
|---|---|---|
| IPR010065 | Domain | Amino acid ABC transporter, permease protein, 3-TM domain |
