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LACCA:K0N3B2
Contents
| Species (Taxon ID) | Lactobacillus casei W56. (1215914) | |
| Gene Name(s) | No Information Provided. | |
| Protein Name(s) | Uncharacterized protein (ECO:0000313 with EMBL:CCK21922.1) | |
| External Links | ||
| UniProt | K0N3B2 | |
| EMBL | HE970764 | |
| RefSeq | WP_012491268.1 | |
| EnsemblBacteria | CCK21922 | |
| KEGG | lcw:BN194_09750 | |
| Proteomes | UP000003734 | |
| InterPro | IPR008044 | |
| Pfam | PF05382 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004175 |
endopeptidase activity |
ECO:0000314 |
F |
Fig. 3B and Table 3 show the hydrolytic specificity of recombinant pure Lc-Lys-2 on L. casei-purified Peptidoglycan (PG). The PG fragments obtained by digestion with Lc-Lys-2 was separated by RP-HPLC and analyzed by MALDI-TOF mass spectrometry. The HPLC profile reveal the hydrolytic specificities for Lc-Lys-2. MS analysis of the major peaks and comparison of the obtained masses with the reference L. casei PG structure enabled identification of peptides generated by Lc-Lys-2 (Table 3) and to deduce the cleavage specificity (Fig. 3D). Lc-Lys-2 has a gamma-D-glutamyl-L-lysyl endopeptidase specificity. |
complete | |||||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Regulski, K et al. (2013) A novel type of peptidoglycan-binding domain highly specific for amidated D-Asp cross-bridge, identified in Lactobacillus casei bacteriophage endolysins. J. Biol. Chem. 288 20416-26 PubMed GONUTS page
