| Comment | This subfamily includes the well-studied secreted O-sialoglycoprotein endopeptidase (glycoprotease, EC 3.4.24.57) of Pasteurella haemolytica, a pathogen. A member from Riemerella anatipestifer, associated with cohemolysin activity, likewise is exported without benefit of a classical signal peptide and shows glycoprotease activity on the test substrate glycophorin. However, archaeal members of this subfamily show unrelated activities as demonstrated in Pyrococcus abyssi: DNA binding, iron binding, apurinic endonuclease activity, genomic association with a kinase domain, and no glycoprotease activity. This family thus pulls together a set of proteins as a homology group that appears to be near-universal in life, yet heterogeneous in assayed function between bacteria and archaea. |
| References | DR PROSITE; PDOC00779; GLYCOPROTEASE
AL clustalw, belvu
DR HAMAP; MF_01447; 21 of 21
RN [1]
RM PMID:1885539
RT Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.
RA Abdullah KM, Lo RY, Mellors A
RL J Bacteriol. 1991 Sep;173(18):5597-603.
RN [2]
RM PMID:17766251
RT An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro.
RA Hecker A, Leulliot N, Gadelle D, Graille M, Justome A, Dorlet P, Brochier C, Quevillon-Cheruel S, Le Cam E, van Tilbeurgh H, Forterre P
RL Nucleic Acids Res. 2007;35(18):6042-51.
RN [3]
RM PMID:11889100
RT Identification and characterization of CAMP cohemolysin as a potential virulence factor of Riemerella anatipestifer.
RA Crasta KC, Chua KL, Subramaniam S, Frey J, Loh H, Tan HM
RL J Bacteriol. 2002 Apr;184(7):1932-9. |
