Types | DnaRegion
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Roles | Coding
CDS
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Sequences | BBa_K888001_sequence (Version 1)
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Description
AIDA-I is synthetized as a 132 kDa pre-protein featuring a signal peptide which is cleaved during transport trough the inner membrane, a 78 kDa adhesin (passenger) domain, and a 45 kDa translocator. This autotransporter has a large capability in translocating relatively large passengers from 12-65 kDa by showing a N-terminal type of fusion (Li et al. 2007; van Bloois et al. 2011). Coupled with a passenger domain and a signal peptide (K888002), it is possible to express functional proteins in the outer membrane of E. coli
van Bloois et al. (2011). Decorating microbes: surface display of proteins on Escherichia coli. Trends Biotechnol. 29(2): 79-86
Li et al. (2007). Presentation of Functional Organophosphorus Hydrolase Fusions on the Surface of Escherichia coli by the AIDA-I Autotransporter Pathway Biotechnol Bioeng. 99(2): 485-90
Notes
Since the fusion of a passenger domain whit AIDA-I translocator domain, it is required a signal peptide for the passenger expression in the outer membrane
Source
E. coli