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The Phosphate-selective porin O and P Family [Function: Specific diffusion channels] Seed alignment | Full alignment | Pfam page | Pfam Wiki page | TC-DB page

This family is comprised by proteins similar to the phosphate-selective porins O and P, which are found mainly in Pseudomonas aeruginosa. These anion-specific porins possess a binding site that has a higher affinity to phosphate than chloride ions. Porin O (OprO) has a higher affinity to polyphosphates, while porin P (OprP) has a higher affinity to orthophosphate. In Pseudomonas aeruginosa, porin O was found to be expressed only under phosphate-starvation conditions during the stationary growth phase. The crystal structure of OprP has revealed a 16-stranded ß-barrel similar to other general diffusion porins.


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Literature references


Probing transport of fosfomycin through substrate specific OprO and OprP from Pseudomonas aeruginosa
Biochem Biophys Res Commun. 2018 Jan 1;495(1):1454-1460. doi: 10.1016/j.bbrc.2017.11.188. Epub 2017 Dec 6.
PMID: 29198700

Structure, function and regulation of Pseudomonas aeruginosa porins
FEMS Microbiol Rev. 2017 Sep 1;41(5):698-722. doi: 10.1093/femsre/fux020.
PMID: 28981745

Conversion of OprO into an OprP-like Channel by Exchanging Key Residues in the Channel Constriction
Biophys J. 2017 Aug 22;113(4):829-834. doi: 10.1016/j.bpj.2017.07.004.
PMID: 28834719

Why do the outer membrane proteins OmpF from E. coli and OprP from P. aeruginosa prefer trimers? Simulation studies
J Mol Graph Model. 2016 Apr;65:1-7. doi: 10.1016/j.jmgm.2016.02.002. Epub 2016 Feb 10.
PMID: 26895142

Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa
Biophys J. 2015 Oct 6;109(7):1429-38. doi: 10.1016/j.bpj.2015.07.035.
PMID: 26445443

Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: effects of charge and solvation
Biochemistry. 2013 Aug 20;52(33):5522-32. doi: 10.1021/bi400522b. Epub 2013 Aug 9.
PMID: 23875754

An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
Nat Struct Mol Biol. 2007 Jan;14(1):85-7. doi: 10.1038/nsmb1189. Epub 2006 Dec 24.
PMID: 17187075

Anion transport through the phosphate-specific OprP-channel of the Pseudomonas aeruginosa outer membrane: effects of phosphate, di- and tribasic anions and of negatively-charged lipids
Biochim Biophys Acta. 1993 Jul 4;1149(2):224-30. doi: 10.1016/0005-2736(93)90205-e.
PMID: 8323941

Polyphosphate-selective porin OprO of Pseudomonas aeruginosa: expression, purification and sequence
Mol Microbiol. 1992 Aug;6(16):2319-26. doi: 10.1111/j.1365-2958.1992.tb01407.x.
PMID: 1406271

The bacterial porin superfamily: sequence alignment and structure prediction
Mol Microbiol. 1991 Sep;5(9):2153-64. doi: 10.1111/j.1365-2958.1991.tb02145.x.
PMID: 1662760

Proteins in this family with 3D-structure
View Entry
Description
Organism
Length
# strands
Outer membrane protein A
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM14847 / LMG 12228 / 1C / PRS 101 / PAO1)
440
16
Bacteriophage adsorption protein A
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM14847 / LMG 12228 / 1C / PRS 101 / PAO1)
438
16


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