Literature summary for 3.4.23.49 extracted from

Hui, C.Y.; Guo, Y.; Liu, L.; Zheng, H.Q.; Wu, H.M.; Zhang, L.Z.; Zhang, W.
Development of a novel bacterial surface display system using truncated OmpT as an anchoring motif (2019), Biotechnol. Lett., 41, 763-777 .

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of the chimeric C-terminally His-tagged and mCherry fluorescence-tagged surface anchor Lpp-OmpT (LOT) in Escherichia coli strain BL21(DE3)	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09169	-	-

Synonyms

Synonyms	Comment	Organism
ompT	-	Escherichia coli
outer membrane protease	-	Escherichia coli

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Release 2023.1 (January 2023)