|PROSITE documentation PDOC00416 [for PROSITE entry PS00448]|
Gram-positive, thermophilic anaerobes such as Clostridium thermocellum or Clostridium cellulolyticum secretes a highly active and thermostable cellulase complex (cellulosome) responsible for the degradation of crystalline cellulose [1,2]. The cellulosome contains at least 30 polypeptides, the majority of the enzymes are endoglucanases (EC 220.127.116.11), but there are also some xylanases (EC 18.104.22.168), β-glucosidases (EC 22.214.171.124) and endo-β-1,3-1,4-glucanases (EC 126.96.36.199).
Complete sequence data for many of these enzymes has been obtained. A majority of these proteins contain a highly conserved region of about 65 to 70 residues which is generally (but not always) located in the C-terminus. This region contains a duplicated segment of 24 amino acids. The function of this duplicated segment is not yet known, although it has been suggested that it could be involved in substrate-binding or in calcium-binding .
Currently this domain has been found in:
The pattern we developed spans the first 20 positions of the 24 amino acids segment.Expert(s) to contact by email:
November 1997 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|Title||Molecular biology of cellulose degradation.|
|Source||Annu. Rev. Microbiol. 44:219-248(1990).|
|2||Authors||Beguin P., Millet J., Aubert J.-P.|
|Title||Cellulose degradation by Clostridium thermocellum: from manure to molecular biology.|
|Source||FEMS Microbiol. Lett. 79:523-528(1992).|
|3||Authors||Chauvaux S., Beguin P., Aubert J.-P., Bhat K.M., Gow L.A., Wood T.M., Bairoch A.|
|Title||Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D.|
|Source||Biochem. J. 265:261-265(1990).|
|4||Authors||Gerngross U.T., Romaniec M.P.M., Kobayashi T., Huskisson N.S., Demain A.L.|
|Title||Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology.|
|Source||Mol. Microbiol. 8:325-334(1993).|