Functional characterisation of Lp_2714, an EAL-domain protein from Lactobacillus plantarum
| Autor: | Richard Charles Brown, Andrew P. Morby, Julian R. Marchesi |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Cyclic di-GMP
Polysaccharide synthesis Molecular Sequence Data Cell Biophysics Protein Sorting Signals Biology Biochemistry chemistry.chemical_compound Bacterial Proteins Sequence Analysis Protein Lactobacillus EAL domain medicine Amino Acid Sequence Molecular Biology Polysaccharides Bacterial Membrane Proteins Phosphodiesterase Cell Biology biology.organism_classification Molecular biology Protein Structure Tertiary medicine.anatomical_structure chemistry Heterologous expression Genome Bacterial Lactobacillus plantarum |
| Zdroj: | Biochemical and Biophysical Research Communications. 411:132-136 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2011.06.112 |
| Popis: | Bioinformatic analysis of lp_2714 from Lactobacillus plantarum WCFS1 demonstrates that it encodes an EAL-domain protein associated with a membrane targeting signal-sequence. Comparison of the predicted primary amino-acid sequence of Lp_2714 shows that it lacks critical catalytic residues and heterologous expression has determined that it does not encode a functional phosphodiesterase. We designate Lp_2714 as a class-3 EAL domain protein probably involved in regulating polysaccharide synthesis on the cell surface the cell. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect