BBa_K1393003

BBa_K1393003 Version 1

Component

Source:
http://parts.igem.org/Part:BBa_K1393003
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Jiajun Tan
Date created: 2014-10-09 11:00:00
Date modified: 2015-05-08 01:10:15

outer membrane porin protein C from Escherichia coli BL21(DE3)



Types
DnaRegion

Roles
Coding

CDS

Sequences BBa_K1393003_sequence (Version 1)

Description

One OmpC molecule consists of 16 transmembrane, antiparallel β-strands, which produce a β-barrel structure surrounding a large channel and are connected by seven internal loops and eight external loops. Three OmpC molecules form a pore structure on the outer membrane of an E.coli cell, which allows small hydrophilic molecules to pass through.

Notes

In general, the amino acid sequences of the external loops are less conservative, and thus these loops may be relatively tolerant to insertion and deletion. We used the external loop as the point of insertion for foreign peptides (copper binding polypeptide or polyhistidine) for cell surface display.

Source

This part is from genome of Escherichia coli BL21(DE3).

Sequence Annotation Location Component / Role(s)
A to G
A to G
G to A
222,223
378,379
731,732
feature/s_mutation point_mutation
feature/s_mutation point_mutation
point_mutation feature/s_mutation
igem#sampleStatus
In stock
igem#status
Available
 
synbiohub#ownedBy
user/james
 
synbiohub#ownedBy
user/myers
 
synbiohub#topLevel
BBa_K1393003/1