HMM Summary Page: TIGR00181
Accession | TIGR00181 |
Name | pepF |
Function | oligoendopeptidase F |
Gene Symbol | pepF |
Trusted Cutoff | 490.55 |
Domain Trusted Cutoff | 490.55 |
Noise Cutoff | 382.10 |
Domain Noise Cutoff | 382.10 |
Isology Type | equivalog |
EC Number | 3.4.24.- |
HMM Length | 591 |
Mainrole Category | Protein fate |
Subrole Category | Degradation of proteins, peptides, and glycopeptides |
Gene Ontology Term | GO:0004222: metalloendopeptidase activity molecular_function |
GO:0006508: proteolysis biological_process | |
Author | Haft DH |
Entry Date | Apr 20 1999 2:09PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This family represents the oligoendopeptidase F clade of the family of larger M3 or thimet (for thiol-dependent metallopeptidase) oligopeptidase family. Lactococcus lactis PepF hydrolyzed peptides of 7 and 17 amino acids with fairly broad specificity. The homolog of lactococcal PepF in group B Streptococcus was named PepB (PMID:8757883), with the name difference reflecting a difference in species of origin rather activity; substrate profiles were quite similar. Differences in substrate specificity should be expected in other species. The gene is duplicated in Lactococcus lactis on the plasmid that bears it. A shortened second copy is found in Bacillus subtilis. |
References | RN [1] RM 7798200 RT Biochemical and genetic characterization of PepF, an oligopeptidase from Lactococcus lactis. RA Monnet V, Nardi M, Chopin A, Chopin MC, Gripon JC. RL J Biol Chem 269, 32070-32076, 1994; RT Biochemical and genetic characterization of PepF, an oligopeptidase from Lactococcus lactis. RN [2] RM 8757883 RT Characterization of PepB, a group B streptococcal oligopeptidase. RA Lin B, Averett WF, Novak J, Chatham WW, Hollingshead SK, Coligan JE, Egan ML, Pritchard DG. RL Infect Immun. 1996 Aug;64(8):3401-6. SE TIGR |