Identification of a cell-bound extracellular protease overproduced by Sulfolobus solfataricus in peptide-rich media.
A new protease, named SsMTP was identified from the archeon Sulfolobus solfataricus. The enzyme is associated to the cell-membrane and over-produced in response to the peptide-enriched media. SsMTP has a molecular mass of 120 kDa showing optimal activity at pH 2.0 in the temperature range 70 - 90 degrees C, and a half-life of 20 days at 80 degrees C. Primary structure analysis revealed that SsMTP represents a novel type of multi-domain thermopsin-like protease containing the catalytic domain followed by two distinct domains, PKD and Y_Y_Y, which are usually involved in a range of protein-protein interactions among the extracellular proteins.
Cannio
Raffaele
R
IBP-Consiglio Nazionale delle Ricerche, Via Pietro Castellino 111, 80131 Napoli, Italy.
Catara
Giuliana
G
Fiume
Imma
I
Balestrieri
Marco
M
Rossi
Mosè
M
Palmieri
Gianna
G
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry; D005780:Gelatin / Q000737:chemistry / Q000378:metabolism; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000096:biosynthesis* / Q000737:chemistry; D010455:Peptides / Q000378:metabolism; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D003470:Culture Media; D008565:Membrane Proteins; D010455:Peptides; D005780:Gelatin; D010450:Endopeptidases; D010447:Peptide Hydrolases; C062465:thermopsin