Part:BBa_K4380001

OmpA signalling sequence

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

Introduction

Vilnius-Lithuania Igem 2022 project NanoFind used this part as a way to expose proteins onto the bacterial surface. The team was working to create an easily accessible nanoplastic detection tool, using peptides, whose interaction with nanoplastic particles would lead to an easily interpretable response. The system itself focused on smaller protein molecules, peptides, which are modified to acquire the ability to connect to the surface of synthetic polymers – plastics. The detection system works when peptides and nanoplastic particles combine and form a sandwich complex - one nanoplastic particle is surrounded by two peptides, attached to their respective protein. The sandwich complex consisted of two main parts – one is a peptide bound to a fluorescent protein, another peptide is immobilized on a cellulose membrane by a cellulose binding domain. A bacterial cell surface display system was used as a novel way to expose the same peptides onto the bacterial membrane, allowing to try to amplify the signal and to find novel peptides by using a peptide evolution protocol.

Usage

OmpA signal peptide is a 20-residue peptide fragment of the 23-residue OmpA signal sequence cleavable by signal peptidase I. This part can be used as a signaling peptide for bacterial surface display proteins to expose on bacterial surface membrane.

Reference

Movva, N. R., Nakamura, K., & Inouye, M. (1980). The amino acid sequence of the signal peptide of ompA protein, a major outer membrane protein of Escherichia coli. The Journal of Biological Chemistry, 255(1), 27–29.