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BPPHE:A8E261
Contents
| Species (Taxon ID) | Enterococcus phage phiEF24C (Enterococcus bacteriophage phi-EF24C). (442493) | |
| Gene Name(s) | No Information Provided. | |
| Protein Name(s) | Putative N-acetylmuramoyl-L-alanine amidase (ECO:0000313 with EMBL:BAF81277.1) | |
| External Links | ||
| UniProt | A8E261 | |
| EMBL | AP009390 | |
| RefSeq | YP_001504118.1 | |
| ProteinModelPortal | A8E261 | |
| GeneID | 5666449 | |
| KEGG | vg:5666449 | |
| Proteomes | UP000001151 | |
| GO | GO:0008745 GO:0009253 | |
| CDD | cd06583 | |
| Gene3D | 3.40.80.10 | |
| InterPro | IPR002502 | |
| Pfam | PF01510 | |
| SMART | SM00644 | |
| SUPFAM | SSF55846 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0008745 |
N-acetylmuramoyl-L-alanine amidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
| GO:0008745 |
N-acetylmuramoyl-L-alanine amidase activity |
ECO:0000315 |
F |
Figure 5: It was previously proven, in the same paper, that orf9 is a N-acetylmuramoyl-L-alanine amidase, but it wasn't known what regions of orf9 was imporant for the lytic activity. To determine the regions of orf9 that are functionally important the researchers constructed eight mutants of the orf9 (of E. faecalis phage φEF24C) by deleting the N-terminal and C-terminal domains (Figure 1A). Only three of the C-terminal deleted mutants were viable (they were soluble), but none of the N-terminal regions were soluble which would indicate that the N-terminal region is required for stability. The C-terminal mutants had their lytic activities were tested by measuring the turbidity, but only the full length orf9, with a Histidine tag, displayed lytic activity. This demonstrated that the full length, N-terminal and C-terminal, orf9 is required for solubilty and lytic activity. |
complete | |||||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Uchiyama, J et al. (2011) Characterization of lytic enzyme open reading frame 9 (ORF9) derived from Enterococcus faecalis bacteriophage phiEF24C. Appl. Environ. Microbiol. 77 580-5 PubMed GONUTS page
