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Journal of Bacteriology, August 1998, p. 3741-3749, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

C. Baldermann,1 A. Lupas,2 J. Lubieniecki,1 and H. Engelhardt1,*

Max-Planck-Institut für Biochemie, Molekulare Strukturbiologie, D-82152 Martinsried, Germany,1 and SmithKline Beecham Pharmaceuticals, Collegeville, Pennsylvania 19426-09892

Received 2 April 1998/Accepted 30 May 1998

Omp21, a minor outer membrane protein of the soil bacterium Comamonas acidovorans, was purified from a spontaneous mutant lacking a surface layer and long-chain lipopolysaccharide. Omp21 synthesis is enhanced by oxygen depletion, and the protein has a variable electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to its heat-modifiable behavior. The structural gene omp21 encodes a precursor of 204 amino acids with a putative signal peptide of 21 amino acids. Mature Omp21 is a typical outer membrane protein with a high content of beta  structure as determined by infrared spectroscopy. Sequence comparisons show that it belongs to a new outer membrane protein family, characterized by eight amphipathic beta  strands, which includes virulence proteins, such as the neisserial opacity proteins, Salmonella typhimurium Rck, and Yersinia enterocolitica Ail, as well as the major outer membrane proteins OmpA from Escherichia coli and OprF from Pseudomonas aeruginosa.

* Corresponding author. Mailing address: Max-Planck-Institut für Biochemie, Molekulare Strukturbiologie, Am Klopferspitz 18a, D-82152 Martinsried, Germany. Phone: 49-89 8578 2650. Fax: 49-89 8578 2641. E-mail: engelhar{at}biochem.mpg.de.

Journal of Bacteriology, August 1998, p. 3741-3749, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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