|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 184.108.40.206), but there are also some xylanases (EC 220.127.116.11), β-glucosidases (EC 18.104.22.168) and endo-β-1,3-1,4-glucanases (EC 22.214.171.124).
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).|