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J Bacteriol. 1991 April; 173(7): 2196-2205

research-article

Nucleotide and derived amino acid sequences of the major porin of Comamonas acidovorans and comparison of porin primary structures.

S Gerbl-Rieger, J Peters, J Kellermann, F Lottspeich and W Baumeister

Max-Planck Institut für Biochemie, Martinsried bei München, Federal Republic of Germany.

ABSTRACT

The DNA sequence of the gene which codes for the major outer membrane porin (Omp32) of Comamonas acidovorans has been determined. The structural gene encodes a precursor consisting of 351 amino acid residues with a signal peptide of 19 amino acid residues. Comparisons with amino acid sequences of outer membrane proteins and porins from several other members of the class Proteobacteria and of the Chlamydia trachomatis porin and the Neurospora crassa mitochondrial porin revealed a motif of eight regions of local homology. The results of this analysis are discussed with regard to common structural features of porins.

J Bacteriol. 1991 April; 173(7): 2196-2205




This article has been cited by other articles:

  • Nikaido, H. (2003). Molecular Basis of Bacterial Outer Membrane Permeability Revisited. Microbiol. Mol. Biol. Rev. 67: 593-656 [Abstract] [Full Text]  
  • Baldermann, C., Lupas, A., Lubieniecki, J., Engelhardt, H. (1998). The Regulated Outer Membrane Protein Omp21 from Comamonas acidovorans Is Identified as a Member of a New Family of Eight-Stranded beta -Sheet Proteins by Its Sequence and Properties. J. Bacteriol. 180: 3741-3749 [Abstract] [Full Text]  


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