Secretary component proteins (SP1) is highly conserved in Salmonella Typhi outer membrane, it modulate host pathogen interaction that is highly conserved in bacterial outer membrane. The molecular mechanism of pathogenicity is complex and these proteins have a wide range of biological functions from host cell toxicity production and block different signaling pathways. Furthermore, our study is to identify molecular characteristic of SP1 component signaling molecules interplay pathogenicity, molecular interactions, sequence assembly and structural organization and drug binding interactions need to understand. Using Computational drug discovery methods to understand the disease targeted virulence factors in SP1 protein should provide new insight into the new evolution of bacterial pathogenesis which could lead to the development of novel therapeutic drug molecules. Here, we report SP-1 component SopE2, SipA, SopA and SopB proteins in disease pathogenesis and reported the antibacterial drugs that inhibit the disease progression and used as a potential drugs.