Pathogens use the needle shaped Type III secretion system to inject effector proteins into the host cell. The effector proteins evade the immune system of the host and help in bacterial colonization. Many effector proteins alter the host cellular target like the cytoskeleton or membrane and bring about necrosis. Thus the identification of effectors is a crucial step in understanding the pathogenesis of the organism. The Type III secretion system of Vibrio vulnificus, which is a marine bacteria causing infection in human beings, has not been studied. The motive of the present study was to identify the effector protein by its amino terminal signal peptide and study its predicted 3-D structure by bioinformatics tools. Homology modeling was carried out by SWISS MODEL server to reveal a helix coiled-coil domain which are associated with the Type III secretion system. Motif analysis revealed probable tyrosine phosphorylation with Phosphoinositide 3-kinase binding motif (MxxY motif) usually occurring in Toll-Like Receptors signaling pathway. The functional annotation of the type III secreted effector protein of V. vulnificus may throw some light on the mechanism of virulence of the organism.