Browse Text search Protein search Domain search Download User manual Related links Citation & Contact


The Outer Membrane Porin (OprD) Family [Function: Specific channels] Seed alignment | Full alignment in OMPdb

The OprD family includes a number of porins in Pseudomonas species and other Gram-negative bacteria that appear to exhibit a variety of substrate specificities. OprD facilitates the diffusion of basic amino acids as well as some structurally analogous beta-lactam antibiotics like imipenem. Mutational inactivation of the oprD gene is associated with carbapenem resistance in Pseudomonas aeruginosa, whereas the C-terminal portion of OprD and, in particular, the hypothetical loop L7, was responsible for the unusual meropenem hypersusceptibility. There is also evidence that OprD porin of Pseudomonas aeruginosa bears protease activity with the catalytic activity established in residues His156, Asp208, and Ser296. However, not all family members have these residues conserved, suggesting that are not all enzymes. Various proteins of the family have shown different specificities in the uptake of metabolites including glycine-glutamate, histidine, proline, tyrosine, cis-aconitate and pyroglutamate. X-ray crystal structure of OprD from Pseudomonas aeruginosa has revealed a monomeric 18-stranded ß-barrel.


Specify pHMMs' % coverageUnspecified More than   
Representative image:  fam_img

Literature references

Analysis of the Pseudomonas aeruginosa oprD gene from clinical and environmental isolates
Environ Microbiol. 2002 Dec;4(12):872-82. doi: 10.1046/j.1462-2920.2002.00281.x.
PMID: 12534469

Function of pseudomonas porins in uptake and efflux
Annu Rev Microbiol. 2002;56:17-38. doi: 10.1146/annurev.micro.56.012302.160310. Epub 2002 Jan 30.
PMID: 12142471

C-terminal region of Pseudomonas aeruginosa outer membrane porin OprD modulates susceptibility to meropenem
Antimicrob Agents Chemother. 2001 Jun;45(6):1780-7. doi: 10.1128/AAC.45.6.1780-1787.2001.
PMID: 11353625

Amino acid-mediated induction of the basic amino acid-specific outer membrane porin OprD from Pseudomonas aeruginosa
J Bacteriol. 1999 Sep;181(17):5426-32. doi: 10.1128/JB.181.17.5426-5432.1999.
PMID: 10464217

Identification of the catalytic triad of the protein D2 protease in Pseudomonas aeruginosa
Biochem Biophys Res Commun. 1998 Jun 9;247(1):142-5. doi: 10.1006/bbrc.1998.8745.
PMID: 9636669

Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa
J Bacteriol. 2006 Jan;188(1):45-54. doi: 10.1128/JB.188.1.45-54.2006.
PMID: 16352820

Structural insight into OprD substrate specificity
Nat Struct Mol Biol. 2007 Nov;14(11):1108-9. doi: 10.1038/nsmb1304. Epub 2007 Oct 21.
PMID: 17952093

Structure of a putative BenF-like porin from Pseudomonas fluorescens Pf-5 at 2.6 A resolution
Proteins. 2010 Nov 1;78(14):3056-62. doi: 10.1002/prot.22829.
PMID: 20737437

Proteins in this family with 3D-structure

Q9HVS0

Q4KH25

Q9I202

Q9HWK2

Q9HWP4

Q9HY38

Q9I1Q4

Q9HUR5

Q9I5H4

Q9I4U9

Q9I6X0

Q9HZH0

Q9I6P8

G3XDA5

P32722

A0A0D5YI36

A0A0D5YKR4


Elixir UTH dib compgen