Complete genome sequence of Vibrio sinus, a potential contributor to collagen degradation.

Collagenase is an enzyme that has been shown to be highly effective in the degradation of both native triple-helical collagen and its denatured form (e.g., gelatin). As a virulence factor secreted by pathogenic bacteria (Clostridium histolyticum, Vibrio, Bacillus cereus), this efficacy is attributed to the unique ability of the enzyme to hydrolyze Gly-X-Y bonds within thermally stable fibrillar structures. A highly efficient gelatin degrading strain, Vibrio sinus S4M6T, was isolated from the surface seawater collected in Dongshan Bay (Fujian, PR China), but the key genes involved in gelatin degradation remain unknown. Here, we report the complete genome sequence of Vibrio sinus S4M6T and its collagen degrading genes. The genome of strain S4M6T consists of two circular chromosomes, with a total chromosome length of 4.78 Mbp and a GC content of 43.4 %. Genomic analysis revealed that strain S4M6T encodes a collagenase gene involved in collagen degradation. This study provides a genetic insight of collagen degradation in marine Vibrio species.