Difference between revisions of "Part:BBa K1978000"

Revision as of 11:47, 18 October 2016

TorA-BtuF

The TorA-BtuF Biobrick consists of a TorA signal sequence linked to BtuF, a protein capable of binding vitamin B12. The TorA signal peptide allows export of fully-folded proteins through the inner membrane via the Tat (Twin-Arginine translocation) system. This construct thus enables export of vitamin B12 bound to BtuF out of the cytoplasm. The TorA sequence codes for an amino-terminal signal peptide that harbours a twin-arginine motif. This motif is vital for the recognition by the Tat system. Moreover, an AxA motif is present, which leads to cleavage by the leader peptidase I (Palmer & Berks 2012).

MNNNDLFQASRRRFLAQLGGLTVAGMLGPSLLTPRRATA

BtuF is the periplasmic binding protein relevant for uptake of vitamin B12 through the outer membrane that is associated with the ABC transporter BtuCD (Kandt et al., 2006). BtuF is the periplasmic binding protein. It has a size of 30.19 kDa and is composed of two globular domains, between which vitamin B12 is bound, linked by a rigid interdomain α-helix (Karpowich et al., 2003).

The TorA signal sequence and the sequence for BtuF are connected by a long linker.

Sequence and Features