title: The major Aeromonas veronii outer membrane protein: gene cloning and sequence analysis.
abstract: The gene encoding the major outer membrane protein (OMP) from Aeromonas veronii, Omp38, was cloned and characterized. Sequence analysis revealed an open reading frame of 1,047 nucleotides coding for a primary protein of 349 amino acids with a 20-amino-acid signal peptide at the N-terminal and the consensus sequence Ala-X-Ala (Ala-Asn-Ala) as the signal peptidase I recognition site. The mature protein is composed of 329 amino acids with a calculated molecular mass of 36,327 Da. The degree of identity of the deduced Omp38 amino acid sequence to porins from enteric bacteria (OmpF, PhoE, and OmpC) was only 30%. Nevertheless, Omp38 possesses typical features of Gram-negative porins, including acidic pI, high glycine and low proline content, no cysteine residues, and a carboxy-terminal Phe. On the basis of PhoE-OmpF three-dimensional structure and the Kyte-Doolittle hydrophobicity analysis, it seems likely that Omp38 secondary structure consists of 16 antiparallel beta-strands and 8 loops. Phylogenetic analyses among Omp38 and related porins from Gram-negative bacteria originate well-defined clusters that agree with the taxonomy of the corresponding organisms.
authors.affiliation: Departamento de Patología Marina, Centro de Investigaciones Biológicas del Noroeste, Av. Mar Bermejo 195, Col. Playa Palo Santa Rita, P. O. Box 128, La Paz, BCS, México. cvazquez04@cibnor.mx
authors.forename: Roberto Carlos
authors.initials: RC
authors.lastname: Vázquez-Juárez
authors.forename: Marta
authors.initials: M
authors.lastname: Gómez-Chiarri
authors.forename: Hugo
authors.initials: H
authors.lastname: Barrera-Saldaña
authors.forename: Norma
authors.initials: N
authors.lastname: Hernández
authors.forename: Felipe
authors.initials: F
authors.lastname: Ascencio
mesh_terms: D000333:Aeromonas / Q000235:genetics*; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003545:Cysteine / Q000235:genetics; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016366:Open Reading Frames; D010649:Phenylalanine / Q000235:genetics; D010802:Phylogeny; D018272:Porins / Q000235:genetics; D011392:Proline / Q000235:genetics; D021382:Protein Sorting Signals; D017433:Protein Structure, Secondary; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
chemical_list: D001425:Bacterial Outer Membrane Proteins; D004269:DNA, Bacterial; D018272:Porins; D021382:Protein Sorting Signals; D010649:Phenylalanine; D011392:Proline; D003545:Cysteine