Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus: a genomic survey

• Published in: Archives of microbiology Vol. 177; no. 3; pp. 209 - 216
• Main Authors: ALBERS, Sonja-Verena, DRIESSEN, Arnold J. M
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 01.03.2002; Berlin
• Subjects: Amino Acid Sequence; Archaea; Archaeal Proteins - chemistry; Archaeal Proteins - genetics; Bacteriology; Biological and medical sciences; Escherichia coli Proteins; Fimbriae Proteins; Fundamental and applied biological sciences. Psychology; Genome, Archaeal; Lipoproteins - chemistry; Lipoproteins - genetics; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Transport Proteins - chemistry; Membrane Transport Proteins - genetics; Microbiology; Molecular Sequence Data; Permeability, membrane transport, intracellular transport; Protein Sorting Signals - genetics; Proteome - chemistry; Sequence Alignment; Sulfolobus - genetics; Sulfolobus - metabolism; Sulfolobus solfataricus; Pilin; Leader peptide; Archaeobacteria; Pilus; Review; Lipoprotein; Sulfolobus solfataricus; Sulfolobaceae; Arginine; Secretory protein; Bacteria; Receptor protein; Sulfolobales
• ISSN: 0302-8933; 1432-072X
• DOI: 10.1007/s00203-001-0386-y

Analysis of the recently completed genome sequence of the thermoacidophilic archaeon Sulfolobus solfataricus reveals that about 4.2% of its proteome consists of putative secretory proteins with signal peptides. This includes members of the four major classes of signal peptides: secretory signal peptides, twin-arginine signal peptides, possible lipoprotein precursors, and type IV pilin signal peptides. The latter group is surprisingly large compared to the size of the groups in other organisms and seems to be used predominately for a subset of extracellular substrate-binding proteins.