Oops!
https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Threonine peptidases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. The threonine peptidases belong to clan PB or are unassigned, clan T-. The type example for this clan is the archaean proteasome beta component of Thermoplasma acidophilum.This entry represents Proteasome subunit beta from Streptomyces coelicolor and similar proteins of found predominantly in Actinobacteria [ ]. PSB is a component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. In Mycobacterium tuberculosis, the proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues [ ]. In complex with the ATPase Mpa, it degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup) []. It is essential for persistence of the pathogen during the chronic phase of infection in the host [, ] and may also function to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities []. It has been related to the resistance of this bacteria to antimicrobial antifolates via regulating both folate reduction and cytokinin production [].Members of this protein family are threonine peptidases belonging to MEROPS peptidase family T1 (clan PB(T)), subfamily T1A. | Name | Proteasome subunit beta, actinobacteria |
| Short Name | PSB_actinobac | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
