1.B.5.1.1
Outer membrane phosphate-selective porin OprP (PorP) of 440 aas. Binds and transports a variety of mono, di- and trivalent anions (Benz et al. 1993). An arginine in the pore determines the anion selectivity (Modi et al. 2013). Residues involved in anion affinity and a preference for Pi versus P2 have been identified (Modi et al. 2015). Both monomeric and trimeric OprP are belived to maintain
their anion selectivity (Niramitranon et al. 2016). The phosphonic-acid antibiotic fosfomycin is highly permeable through the OprO and OprP channels (Citak et al. 2018).
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| Accession Number: | P05695 |
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| Protein Name: | Porin P |
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| Length: | 440 |
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| Molecular Weight: | 48211.00 |
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| Species: | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [208964] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Cell outer membrane1 / Multi-pass membrane protein2 |
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| Substrate |
anion, phosphate(3-), fosfomycin |
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1: MIRRHSCKGV GSSVAWSLLG LAISAQSLAG TVTTDGADIV IKTKGGLEVA TTDKEFSFKL
61: GGRLQADYGR FDGYYTNNGN TADAAYFRRA YLEFGGTAYR DWKYQINYDL SRNVGNDSAG
121: YFDEASVTYT GFNPVNLKFG RFYTDFGLEK ATSSKWVTAL ERNLTYDIAD WVNDNVGTGI
181: QASSVVGGMA FLSGSVFSEN NNDTDGDSVK RYNLRGVFAP LHEPGNVVHL GLQYAYRDLE
241: DSAVDTRIRP RMGMRGVSTN GGNDAGSNGN RGLFGGSSAV EGLWKDDSVW GLEGAWALGA
301: FSAQAEYLRR TVKAERDRED LKASGYYAQL AYTLTGEPRL YKLDGAKFDT IKPENKEIGA
361: WELFYRYDSI KVEDDNIVVD SATREVGDAK GKTHTLGVNW YANEAVKVSA NYVKAKTDKI
421: SNANGDDSGD GLVMRLQYVF