Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Michael James George Milevskiy
Date created: 2009-09-27 11:00:00
Date modified: 2015-05-08 01:11:23
DnaK is a chaperone protein that assists with polypeptide folding
| Types | DnaRegion |
| Roles | CDS Coding |
| Sequences | BBa_K205002_sequence (Version 1) |
Description
In conjuction with DnaJ and GrpE, DnaK assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaJ, GrpE, GroEL and GroES forms the heat shock system in bacteria.Notes
In order to comply with Standard 23, two restriction sites were removed within the gene. These sites were EcoRI and BglII, which were removed through mutagenesis.Source
Christos Kyratsous Columbia Univ, Coll Phys & Surg, Dept Microbiol, New York, NY 10032 USARef: Kyratsous, CA, Silverstein, SJ, DeLong, CR, Panagiotidis, CA. (2009) "Chaperone-fusion expression plasmid vectors for improved solubility of recombinant proteins in Escherichia coli" GENE VOL: 440 Issue: 1-2 Pages: 9-15 Date: Jul 1 2009
| Sequence Annotation | Location | Component / Role(s) |
| Start of DnaK End of DnaK Mutation from t to g to remove the EcoRI restriction site Mutation from t to c to remove the BglII restriction site | 1,3 1897,1899 730,730 933,933 | feature/start start_codon stop_codon feature/stop point_mutation feature/s_mutation point_mutation feature/s_mutation |