In silico Structural and Functional Characterization of a Hypothetical Protein from Stenotrophomonas maltophilia SRM01

Abstract

Stenotrophomonas maltophilia is a low-virulence opportunistic pathogen that causes human infections, especially in profound ill patients. Even if the bacterial genomes seem understood, the activities of many proteins are unknown. The purpose of our current research is to unravel the functional characteristics i.e. functional domain search and valuable regions of a hypothetical protein that would aid in the identification of potential drug targets in Stenotrophomonas maltophilia. The hypothetical protein of S.maltophilia was located and annotated using different in silico techniques. Our target protein was predicted to be Transcrip Reg superfamily YebC/PmpR based on motif and domain analysis by functional annotation tools. The regulator proteins of the YebC family are part of a vast collection of widely conserved hypothetical proteins with unclear functions. Examining and reviewing the function of YebC family protein, they repress Quorum sensing by directly binding to the promoter region of QS master regulator pqrS. It has also been reported that T3SS expression is regulated by YebC, to activate the virulence expression direct interaction with one of the T3SS promoters is needed.

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“…The grid box was determined by the binding site residues, with all binding site residues fitting within the grid box. The Discovery Studio visualizer program was used to examine the molecular interactions in the complexes in great detail (Koshy et al, 2022).…”