1.B.39 The Bacterial Porin, OmpW (OmpW) Family
OmpW of Salmonella typhimurium has been shown to be required for the efficient efflux of methyl viologen and benzyl viologen (P. Youderian, personal communication). It functions in parallel with OmpD (NmpC in E. coli) which is the major Salmonella porin. OmpW is also the receptor for colicin S4. Homologues are found in many Gram-negative bacterial species including Pseudomonas, Azotobacter, Desulfitobacterium, Burkholderia, Xanthomonas, Rhodobacter, Ralstonia, Delftia and Rickettsia. One homologue is the major outer membrane protein, OprG of Pseudomonas aeruginosa (Gensberg et al., 1999). Another is the outer membrane protein, AlkL, probably involved in alkane transport (van Beilen et al., 1992). An x-ray structure of OmpW has been presented (Albrecht et al. 2006). OmpW exhibits fast internal motion and residual conformational entropy (O'Brien et al. 2020).
This family belongs to the: Outer Membrane Pore-forming Protein I (OMPP-I) Superfamily .
References associated with 1.B.39 family:
Albrecht, R., K. Zeth, J. Söding, A. Lupas, and D. Linke. (2006). Expression, crystallization and preliminary X-ray crystallographic studies of the outer membrane protein OmpW from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 415-418. 16582500
Beketskaia, M.S., D.C. Bay, and R.J. Turner. (2014). Outer membrane protein OmpW participates with small multidrug resistance protein member EmrE in quaternary cationic compound efflux. J. Bacteriol. 196: 1908-1914. 24633876
Benz, R., M.D. Jones, F. Younas, E. Maier, N. Modi, R. Mentele, F. Lottspeich, U. Kleinekathöfer, and J. Smit. (2015). OmpW of Caulobacter crescentus Functions as an Outer Membrane Channel for Cations. PLoS One 10: e0143557. 26606672
Gensberg, K., A.W. Smith, F.S. Brinkman, and R.E. Hancock. (1999). Identification of oprG, a gene encoding a major outer membrane protein of Pseudomonas aeruginosa. J. Antimicrob. Chemother. 43: 607-608. 10350397
Giacani L., Brandt SL., Ke W., Reid TB., Molini BJ., Iverson-Cabral S., Ciccarese G., Drago F., Lukehart SA. and Centurion-Lara A. (2015). Transcription of TP0126, Treponema pallidum putative OmpW homolog, is regulated by the length of a homopolymeric guanosine repeat. Infect Immun. 83(6):2275-89. 25802057
Gil, F., F. Ipinza, J. Fuentes, R. Fumeron, J.M. Villarreal, A. Aspée, G.C. Mora, C.C. Vásquez, and C. Saavedra. (2007). The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar typhimurium. Res. Microbiol. 158: 529-536. 17618087
Kucharska, I., P. Seelheim, T. Edrington, B. Liang, and L.K. Tamm. (2015). OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa. Structure 23: 2234-2245. 26655471
Ladkau, N., M. Assmann, M. Schrewe, M.K. Julsing, A. Schmid, and B. Bühler. (2016). Efficient production of the Nylon 12 monomer ω-aminododecanoic acid methyl ester from renewable dodecanoic acid methyl ester with engineered Escherichia coli. Metab Eng 36: 1-9. [Epub: Ahead of Print] 26969251
Neher, T.M. and D.R. Lueking. (2009). Pseudomonas fluorescens ompW: plasmid localization and requirement for naphthalene uptake. Can. J. Microbiol. 55: 553-563. 19483784
O''Brien, E.S., B. Fuglestad, H.J. Lessen, M.A. Stetz, D.W. Lin, B.S. Marques, K. Gupta, K.G. Fleming, and J.J. Wand. (2020). Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy. Angew Chem Int Ed Engl. [Epub: Ahead of Print] 32277554
Pilsl, H., D. Smajs, and V. Braun. (1999). Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane. J. Bacteriol. 181: 3578-3581. 10348872
Ritter A., Com E., Bazire A., Goncalves Mdos S., Delage L., Le Pennec G., Pineau C., Dreanno C., Compere C. and Dufour A. (2012). Proteomic studies highlight outer-membrane proteins related to biofilm development in the marine bacterium Pseudoalteromonas sp. D41. Proteomics. 12(21):3180-92. 22965736
Sanganna Gari, R.R., P. Seelheim, B. Marsh, V. Kiessling, C.E. Creutz, and L.K. Tamm. (2018). Quaternary structure of the small amino acid transporter OprG from Pseudomonas aeruginosa. J. Biol. Chem. [Epub: Ahead of Print] 30237175
Sullivan, J.T., S.D. Brown, and C.W. Ronson. (2013). The NifA-RpoN regulon of Mesorhizobium loti strain R7A and its symbiotic activation by a novel LacI/GalR-family regulator. PLoS One 8: e53762. 23308282
Tabibpour, N.S., A. Doosti, and A. Sharifzadeh. (2023). Putative novel outer membrane antigens multi-epitope DNA vaccine candidates identified by Immunoinformatic approaches to control Acinetobacter baumannii. BMC Immunol 24: 46. 37980458
Touw, D.S., D.R. Patel, and B. van den Berg. (2010). The crystal structure of OprG from Pseudomonas aeruginosa, a potential channel for transport of hydrophobic molecules across the outer membrane. PLoS One 5: e15016. 21124774
van Beilen, J.B., G. Eggink, H. Enequist, R. Bos, and B. Witholt. (1992). DNA sequence determination and functional characterization of the OCT-plasmid-encoded alkJKL genes of Pseudomonas oleovorans. Mol. Microbiol. 6: 3121-3136.
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Xiao, M., Y. Lai, J. Sun, G. Chen, and A. Yan. (2016). Transcriptional Regulation of the Outer Membrane Porin Gene ompW Reveals its Physiological Role during the Transition from the Aerobic to the Anaerobic Lifestyle of Escherichia coli. Front Microbiol 7: 799. 27303386