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This family consists of homologs to OmpW protein of Salmonella typhimurium, Escherichia coli and Vibrio cholerae (minor outer membrane proteins) and the major outer membrane protein OprG of Pseudomonas aeruginosa. OprG appears to be involved in low-affinity iron uptake, whereas OmpW is also the Receptor for colicin S4. Homologs have been found in many Gram-negative bacterial genera including Azotobacter, Desulfitobacterium, Burkholderia, Xanthomonas, Rhodobacter, Ralstonia, Delftia and Rickettsia. Proteins of the family show low sequence similarity to members of the OprF family, while the structures of both OmpW of Escherichia coli and OprG from Pseudomonas aeruginosa, revealed an 8-stranded ß-barrel.
Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane
J Bacteriol. 1999 Jun;181(11):3578-81. doi: 10.1128/JB.181.11.3578-3581.1999.
Identification of oprG, a gene encoding a major outer membrane protein of Pseudomonas aeruginosa
J Antimicrob Chemother. 1999 Apr;43(4):607-8. doi: 10.1093/jac/43.4.607.
The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel
J Biol Chem. 2006 Mar 17;281(11):7568-77. doi: 10.1074/jbc.M512365200. Epub 2006 Jan 12.
The crystal structure of OprG from Pseudomonas aeruginosa, a potential channel for transport of hydrophobic molecules across the outer membrane
PLoS One. 2010 Nov 29;5(11):e15016. doi: 10.1371/journal.pone.0015016.
|Proteins in this family with 3D-structure|