TatP
TatP predicts twin-arginine (Tat) signal peptides and their potential cleavage sites in bacterial proteins to identify proteins targeted to the periplasmic compartment or extracellular environment via the Tat translocation pathway.
Key Features:
- High accuracy: Correctly classifies 91% of known Tat signal peptides and predicts 84% of annotated cleavage sites.
- Reduction of false positives: Produces fewer false positive predictions compared to simple pattern matching and complementary rule-based methods.
- Discrimination of signal types: Distinguishes Tat signal peptides from cytoplasmic proteins with similar motifs and from Sec signal peptides.
- Hydrophobicity-based artificial neural network: Employs an artificial neural network to separate Tat and Sec signal peptides based on hydrophobicity profiles.
- Data training on known substrates: Trained using sequence data from known Tat substrates to enhance predictive performance.
- Regular expression filtering: Supports filtering of input sequences using Perl syntax regular expressions.
- Cleavage site reporting: Reports potential cleavage sites to inform analyses of protein processing and maturation.
Scientific Applications:
- Tat pathway studies: Identification of Tat substrates for research on the twin-arginine translocation system.
- Protein targeting and translocation analysis: Analysis of signals that direct proteins to the periplasmic compartment or extracellular environment.
- Functional annotation: Distinguishing secreted/periplasmic proteins from cytoplasmic proteins for genome and proteome annotation.
- Microbial physiology and pathogenesis: Investigation of protein localization relevant to microbial physiology and virulence mechanisms.
- Synthetic biology and biotechnology: Selection and validation of signal peptides for engineering secretion or periplasmic localization in bacterial systems.
Methodology:
Sequence data from known Tat substrates were used to train the model; an artificial neural network discriminates Tat versus Sec signal peptides based on hydrophobicity profiles; input sequences can be filtered using Perl syntax regular expressions.
Topics
Details
- License:
- Other
- Maturity:
- Emerging
- Cost:
- Free of charge (with restrictions)
- Tool Type:
- api, web application
- Operating Systems:
- Linux
- Added:
- 1/21/2015
- Last Updated:
- 12/16/2018
Operations
Data Inputs & Outputs
Protein cleavage site prediction
Publications
Bendtsen JD, Nielsen H, Widdick D, Palmer T, Brunak S. Prediction of twin-arginine signal peptides. BMC Bioinformatics. 2005;6(1). doi:10.1186/1471-2105-6-167. PMID:15992409. PMCID:PMC1182353.
Documentation
Links
Software catalogue
http://cbs.dtu.dk/services