(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Corynebacteriales: NE > Corynebacteriaceae: NE > Corynebacterium: NE > Corynebacterium efficiens: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MGAIHHNFTRERLMKLLRRIAAPVAALGIALSTVVAPTAVSAAELTPAAV AGDTPQSTITVGAKYPEQPAPRWRARVNASGERVKEMWAYSPSMDRDVPL VVITADESAGPRPVIYLLNGGDGGEGNANWIMQTDVIDFYLEKNVNVVIP MEGKFSYYTDWVQENAALGGKQMWETFLVKELPGPLEEELNADGQRAIAG MSMSATTSLLFPQHYPGFYDAAASFSGCASTSQPLPWEYIRLTLDRGNAT PEQMWGPRGGEVNIYNDALINSDKLRGTDLYISNASGLAGHWESANSPRF NGLDQAYLSLAMTETIVTGGLIEAATNKCTHDLKAKLDHAGIPADWNLRP TGTHSWGWWQDDLRGSWDTFARSFGLENENA
Corynebacterium efficiens is the closest relative of Corynebacterium glutamicum, a species widely used for the industrial production of amino acids. C. efficiens but not C. glutamicum can grow above 40 degrees C. We sequenced the complete C. efficiens genome to investigate the basis of its thermostability by comparing its genome with that of C. glutamicum. The difference in GC content between the species was reflected in codon usage and nucleotide substitutions. Our comparative genomic study clearly showed that there was tremendous bias in amino acid substitutions in all orthologous ORFs. Analysis of the direction of the amino acid substitutions suggested that three substitutions are important for the stability of the C. efficiens proteins: from lysine to arginine, serine to alanine, and serine to threonine. Our results strongly suggest that the accumulation of these three types of amino acid substitutions correlates with the acquisition of thermostability and is responsible for the greater GC content of C. efficiens.
