GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:24140647
| Citation |
Gutelius, D, Hokeness, K, Logan, SM and Reid, CW (2014) Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination. Microbiology (Reading, Engl.) 160:209-16 |
|---|---|
| Abstract |
Clostridium difficile is the most common cause of enteric disease and presents a major burden on healthcare systems globally due in part to the observed rapid rise in antibiotic resistance. The ability of C. difficile to form endospores is a key feature in the organism's pathogenesis and transmission, and contributes greatly to its resilient nature. Endospores are highly resistant to disinfection, allowing them to persist on hospital surfaces. In order for the organism to cause disease, the spores must germinate and revert to a vegetative form. While spore germination in Bacillus spp. is well understood, very little is known about this process in Clostridia. Here we report the characterization of SleC (CD0551) from C. difficile 630. Bioinformatic analysis of SleC indicated a multi-domained protein possessing a peptidoglycan-binding (PGB) domain, a SpoIID/LytB domain and an undefined N-terminal region. We have confirmed that SleC is an exo-acting lytic transglycosylase with the catalytic activity localized to the N-terminal region. Additionally, we have shown that both the N-terminal catalytic domain and the C-terminal PGB domain require muramyl-δ-lactam for substrate binding. As with carbohydrate-binding modules from cellulases and xylanases, the PGB domain may be responsible for increasing the processivity of SleC by concentrating the enzyme at the surface of the substrate. |
| Links |
PubMed PMC3917228 Online version:10.1099/mic.0.072454-0 |
| Keywords |
Catalytic Domain; Clostridium difficile/enzymology; Clostridium difficile/genetics; Clostridium difficile/growth & development; Computational Biology; Peptidoglycan/metabolism; Peptidoglycan Glycosyltransferase/genetics; Peptidoglycan Glycosyltransferase/metabolism; Protein Binding; Protein Structure, Tertiary; Spores, Bacterial/growth & development |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0008933: lytic transglycosylase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0008933: lytic transglycosylase activity |
ECO:0000314: |
F |
Figure 5 shows the peaks generated by muropeptides produced by the activity of SleC on peptidoglycan. Table 1 lists the muropeptides. |
complete | ||||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
