Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus: a genomic survey.
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.
Albers
Sonja-Verena
SV
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands.
Driessen
Arnold M
AM
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D020745:Genome, Archaeal; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics*; D020543:Proteome / Q000737:chemistry; D016415:Sequence Alignment; D016944:Sulfolobus / Q000235:genetics* / Q000378:metabolism
D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; D020543:Proteome; C408585:twin-arginine translocase complex, E coli; D036781:Fimbriae Proteins