| Accession | TIGR01382 |
| Name | PfpI |
| Function | intracellular protease, PfpI family |
| Trusted Cutoff | 139.05 |
| Domain Trusted Cutoff | 139.05 |
| Noise Cutoff | 112.55 |
| Domain Noise Cutoff | 112.55 |
| Isology Type | subfamily |
| HMM Length | 169 |
| Mainrole Category | Protein fate |
| Subrole Category | Degradation of proteins, peptides, and glycopeptides |
| Gene Ontology Term | GO:0006508: proteolysis biological_process |
| | GO:0008234: cysteine-type peptidase activity molecular_function |
| Author | Haft DH |
| Entry Date | Nov 19 2001 11:02AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. |
| References | RM 11114201
RT Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
RA Du X, Choi IG, Kim R, Wang W, Jancarik J, Yokota H, Kim SH.
RL Proc Natl Acad Sci U S A 2000 Dec 19;97(26):14079-84 |
