Abstract
Streptomyces coelicolor is a gram-positive soil bacterium which is well known for the production of several antibiotics used in various biotechnological applications. But numerous proteins from its genome are considered hypothetical proteins. Therefore, the present study aimed to reveal the functions of a hypothetical protein from the genome of S. coelicolor. Several bioinformatics tools were employed to predict the structure and function of this protein. Sequence similarity was searched through the available bioinformatics databases to find out the homologous protein. The secondary and tertiary structure were predicted and further validated with quality assessment tools. Furthermore, the active site and the interacting proteins were also explored with the utilization of CASTp and STRING server. The hypothetical protein showed the important biological activity having with two functional domain including POD-like_MBL-fold and rhodanese homology domain. The functional annotation exposed that the selected hypothetical protein could show the hydrolase activity. Furthermore, protein-protein interactions of selected hypothetical protein revealed several functional partners those have the significant role for the bacterial survival. At last, the current study depicts that the annotated hypothetical protein is linked with hydrolase activity which might be of great interest to the further research in bacterial genetics.
Highlights
Streptomyces coelicolor A3(2) is one of the best studied representatives amongst other members of the genus Streptomyces [1]
Functional annotation of hypothetical protein revealed it has tremendous quantities of significant biosynthetic gene sets [7,8]. These characteristics have elicited biotechnological interest in this bacterium and have aroused the interest of researchers in the past few years to investigate the different proteins involved in secondary metabolites production
It is recently found that albaflavenone, germicidin A, and chalcone are produced during germination of Streptomyces coelicolor [9] and the genes responsible for the biosynthesis of streptomycete secondary metabolites are generally clustered with high expression of regulation [10]
Summary
Streptomyces coelicolor A3(2) is one of the best studied representatives amongst other members of the genus Streptomyces [1]. It is considered a model organism to study soil bacteria [3], which has been studied genetically for about 60 years [4] They have the capability to degrade chitin and other compounds that are difficult to degrade which makes them especially important [5]. Streptomyces coelicolor A3(2) has the potential to make such secondary metabolites, and metagenomic analysis has revealed it has Ferdous N et al Functional annotation of hypothetical protein revealed it has tremendous quantities of significant biosynthetic gene sets [7,8] These characteristics have elicited biotechnological interest in this bacterium and have aroused the interest of researchers in the past few years to investigate the different proteins involved in secondary metabolites production. When all three genes were absent, clorobiocin, an antibiotic which inhibits the enzyme DNA gyrase was produced only in very small amounts, but when cloY was restored, clorobiocin was produced at a more significant level [11]
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