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