TCDB is operated by the Saier Lab Bioinformatics Group

1.B.31 The Campylobacter jejuni Major Outer Membrane Porin (MomP) Family

Campylobacter jejuni MomP is a trimeric, β -sheet-type porin of 424 aas that packs with different lattice types when reconstituted with lipids. The protein can exist as the native trimer or as a stable monomer, depending in the concentration of sodium dodecyl sulfate. It serves several physiological functions: (1) in the structural organization of the outer membrane, (2) as an adhesin, and (3) as a porin. The monomeric and trimeric porins exhibit similar single channel conductances with the same cation selectivities and the same sensitivities to voltage when reconstituted in an artificial lipid bilayer. A second homologue of MomP with 88% identity to the first one has been sequenced (gbAL139077).

The transport reaction catalyzed by the C. jejuni MomP is:

solutes (out) solutes (periplasm)

This family belongs to the: Porin Superfamily I.

References associated with 1.B.31 family:

Dé, E., M. Jullien, G. Labesse, J.M. Pagès, G. Molle, and J.M. Bolla. (2000). MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein. FEBS Lett. 469: 93-97. 10708763
Zhuang, J., A. Engel, J-M. Pages, and J.M. Bolla (1997). The Campylobacter jejuni porin trimers pack into different lattice types when reconstituted in the presence of lipid. Eur. J. Biochem. 244: 575-579. 9119026