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Currently, no <jats:italic><jats:italic>Legionella<\/jats:italic><\/jats:italic> effectors have been identified at the mitochondrial outer membrane, a critical interface between the organelle and the rest of the cell. We screened the <jats:italic><jats:italic>Legionella<\/jats:italic><\/jats:italic> effector repertoire for features of mitochondrial tail-anchored (TA) proteins and identified four putative TA effectors. Among them, <jats:italic>Lp<\/jats:italic>PIP (Lpg1625) localizes to the mitochondrial outer membrane and interacts with all three isoforms of protein phosphatase 1 (PP1) via an RVxF motif, functioning as a PP1-interacting protein (PIP). Importantly, PP1 remains catalytically active upon interaction with <jats:italic><jats:italic>Lp<\/jats:italic><\/jats:italic>PIP to dephosphorylate mitochondrial outer membrane proteins. Altering the TA signature to direct <jats:italic><jats:italic>Lp<\/jats:italic><\/jats:italic>PIP to the ER induces ER-recruitment of PP1 and dephosphorylation of ER-resident proteins, indicating that <jats:italic><jats:italic>Lp<\/jats:italic><\/jats:italic>PIP controls PP1 localization and not substrate specificity. 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