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The Outer Membrane Protein beta-barrel domain Family [Function: Unknown] Seed alignment | Full alignment in OMPdb | |
This domain is found in a wide range of outer membrane proteins, found mainly in Alphaproteobacteria.Examples are the Major Outer Membrane Protein (ompP1) from various strains of Coxiella burnetti, which possesses the typical porin properties: it is heat-modifiable, it has channel activity and is predicted to form a ß-barrel; Omp3b from Brucella abortus and homologs from various Alphaproteobacteria that are believed to be involved in bacterial surface control and host cell interactions; and proteins from various species of Pseudomonas, of which a 3D structure suggests a ß-barrel structure of 8 stands. | |
Literature references | |
Membrane topology of the outer membrane protein OprH from Pseudomonas aeruginosa: PCR-mediated site-directed insertion and deletion mutagenesis J Bacteriol. 1996 Jun;178(11):3346-9. doi: 10.1128/jb.178.11.3346-3349.1996. PMID: 8655519 | |
Pseudomonas aeruginosa outer membrane protein OprH: expression from the cloned gene and function in EDTA and gentamicin resistance J Bacteriol. 1991 Nov;173(21):6657-64. doi: 10.1128/jb.173.21.6657-6664.1991. PMID: 1938872 | |
Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa J Biol Chem. 2011 Nov 11;286(45):39211-23. doi: 10.1074/jbc.M111.280933. Epub 2011 Aug 24. PMID: 21865172 | |
Temporal analysis of Coxiella burnetii morphological differentiation J Bacteriol. 2004 Nov;186(21):7344-52. doi: 10.1128/JB.186.21.7344-7352.2004. PMID: 15489446 | |
Cloning and porin activity of the major outer membrane protein P1 from Coxiella burnetii Infect Immun. 2002 Dec;70(12):6741-50. doi: 10.1128/iai.70.12.6741-6750.2002. PMID: 12438349 | |
Proteins in this family with 3D-structure | |
Q8D0Z7 | |
Q51486 | |
A0A5P8YI02 |
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