In this study, bioinformatics techniques such as domain search, molecular docking were used to study the relationship between SARS-COV-2 virus ORF7a protein and lipopolysaccharide. The results showed that the transmembrane protein ORF7a protein had ABC transporter domains: ATP binding and ABC transmembrane domains. The ABC transporter domain of ORF7a transported molecules such as metal ions, heme, nucleosides, amino acids and oligopeptides, sugars, vitamins, salts and alkalis, and it had a multi-drug efflux function. ORF7a had domains for synthetic lipopolysaccharide. The lipopolysaccharide synthesized by ORF7a bound to CD14 molecules through LBP protein to activate CD14 + monocytes. The extracellular ORF7a with the N-terminus and C-terminus cut off still had the BPI1 domain (CELYHYQECVR) and two ATP-binding motifs. The first ATP binding site ("HYQEC") is in the BPI1/LBP domain. The second ATP binding site ("TYEGNS") is behind the relative direction of the BPI/LBP domain. Extracellular ORF7a had lipopolysaccharide -binding protein (LBP) -like activity, could be combined with CD14 antigen molecules.