POTRA: A conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins

Trends in Biochemical Sciences

Volumn 28, Issue 10, 2003, Pages 523-526

  Sánchez Pulido, Luis ^a   Devos, Damien ^a,c   Genevrois, Stéphanie ^b   Vicente, Miguel ^a   Valencia, Alfonso ^a  

^a CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^b UNIVERSITY OF NAMUR   (Belgium)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; OUTER MEMBRANE PROTEIN; PROTEIN FTSQ; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; FTSQ PROTEIN, E COLI; MEMBRANE PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; BACILLUS SUBTILIS; BACTERIUM; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE TRANSPORT; CHLOROPLAST; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN TRANSPORT; REVIEW; SEQUENCE HOMOLOGY; ARTICLE; CELL MEMBRANE; CHEMISTRY; ENZYME ACTIVE SITE; METABOLISM; MOLECULAR GENETICS; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CELL MEMBRANE; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT;

EID: 0642377467     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2003.08.003     Document Type: Short Survey

References (25)

1. Jarvis P., Soll J. Toc, tic, and chloroplast protein import. Biochim. Biophys. Acta. 1590:2002;177-189.
2. Konninger U.W., et al. The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes. Mol. Microbiol. 32:1999;1212-1225.
3. Yang F.L., Braun V. ShlB mutants of Serrantia marcescens allow uncoupling of activation and secretion of the ShlA hemolysin. Int. J. Med. Microbiol. 290:2000;529-538.
4. Guedin S., et al. Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 275:2000;30202-30210.
5. Genevrois S., et al. The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane. EMBO J. 22:2003;1780-1789.
6. Voulhoux R., et al. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science. 299:2003;262-265.
7. Reumann S., et al. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc. Natl. Acad. Sci. U. S. A. 96:1999;784-789.
8. Reumann S., Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci. 4:1999;302-307.
9. Errington J., et al. Cytokinesis in bacteria. Microbiol. Mol. Biol. Rev. 67:2003;52-65.
10. Eddy S.R. Profile hidden Markov models. Bioinformatics. 14:1998;755-763.
11. Rost B. PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:1996;525-539.
12. Hinnah S.C., et al. Reconstitution of a chloroplast protein import channel. EMBO J. 16:1997;7351-7360.
13. Stebbins C.E., Galan J.E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature. 414:2001;77-81.
14. Schleiff E., et al. A GTP-driven motor moves proteins across the outer envelope of chloroplasts. Proc. Natl. Acad. Sci. U. S. A. 100:2003;4604-4609.
15. Buchanan S.K., et al. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 6:1999;56-63.
16. Schulz G.E. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta. 1565:2002;308-317.
17. Ruffolo C.G., Adler B. Cloning, sequencing, expression, and protective capacity of the oma87 gene encoding the Pasteurella multocida 87-kilodalton outer membrane antigen. Infect. Immun. 64:1996;3161-3167.
18. Yang Y., et al. A 20-kilodalton N-terminal fragment of the D15 protein contains a protective epitope(s) against Haemophilus influenzae type a and type b. Infect. Immun. 66:1998;3349-3354.
19. Manning D.S., et al. Omp85 proteins of Neisseria gonorrhoeae and Neisseria meningitidis are similar to Haemophilus influenzae D-15-Ag and Pasteurella multocida Oma87. Microb. Pathog. 25:1998;11-21.
20. Cameron C.E., et al. Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92. J. Infect. Dis. 181:2000;1401-1413.
21. Robb C.W., et al. Identification and characterization of an in vivo regulated D15/Oma87 homologue in Shigella flexneri using differential display polymerase chain reaction. Gene. 262:2001;169-177.
22. Poolman J.T., et al. Developing a nontypeable Haemophilus influenzae (NTHi) vaccine. Vaccine. 19:2000;S108-S115.
23. Notredame C., et al. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302:2000;205-217.
24. Nielsen H., et al. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
25. Martelli P.L., et al. A sequence-profile-based HMM for predicting and discriminating β barrel membrane proteins. Bioinformatics. 18:2002;S46-S53.