We have seen that PRP domains are present in the SopA ubiquitination inhibitor whose biochemical function is to bind to TRIM56 and TRIM65 and block the host immune response of interferon production that would normally stimulate proteasome targeting of the bacterial proteins as part of the host immune response to infection; however, the PRP domain of SopA does not directly interact with the targeted TRIM proteins leaving the precise function of the PRP domain of SopA in question. Here, TRIM56 is linked to infection.