ProtScreen
ProtScreen analyzes proteomes from lactic acid bacteria species, including Lactobacilli, Enterococci, Lactococci, Carnobacteria, and Leuconostocs, using sequences from UniProt and NCBI to identify Sortase A Dependent Proteins (SDPs) and characterize LPXTG motifs.
Key Features:
- Proteome scope: Analyzes proteomes from lactic acid bacteria (Lactobacilli, Enterococci, Lactococci, Carnobacteria, Leuconostocs).
- Data sources: Processes genomic and proteomic sequences obtained from UniProt and NCBI.
- SDP identification: Identifies Sortase A Dependent Proteins (SDPs) from input sequences.
- Motif recognition: Recognizes the LPXTG motif critical for sortase A recognition and cleavage and analyzes the X-position variability.
- Frequency analysis: Computes frequency and abundance of amino acids at the X position within the LPXTG motif across LAB strains.
- Docking simulations: Performs docking simulations to assess interaction dynamics between sortase A and SDPs.
Scientific Applications:
- Understanding Probiotic Persistence: Elucidates mechanisms of bacterial attachment to the host intestine via sortase A and SDPs, enhancing understanding of probiotic persistence in the gut.
Methodology:
Extracts data from established databases, performs motif recognition using built-in algorithms, conducts frequency analysis of amino acids in the LPXTG motif, and performs docking simulations to assess interaction dynamics between sortase A and SDPs.
Topics
Details
- Added:
- 1/18/2021
- Last Updated:
- 1/29/2021
Operations
Publications
Javanshir N, Rezvani EM, Mazhary Z, Razani S, Ahmadian G, Fard NA. Proteome Mining of Sortase A Dependent Proteins (SDPs) in Lactic Acid Bacteria and Docking Analysis of SDPs Interaction with Sortase A. Unknown Journal. 2020. doi:10.21203/rs.3.rs-125367/v1.
Javanshir N, Rezvani EM, Mazhary Z, Razani S, Ahmadian G, Allahyari N. Proteome Mining of Sortase A Dependent Proteins (SDPs) in Lactic Acid Bacteria and Docking Analysis of SDPs interaction with Sortase A. Unknown Journal. 2020. doi:10.21203/rs.3.rs-116217/v1.