The study investigates the role of phosphorylation of the autophagy receptor optineurin (OPTN) in the selective autophagy of *Salmonella enterica*. Phosphorylation of OPTN by the protein kinase TANK binding kinase 1 (TBK1) on serine-177 enhances its binding affinity to LC3, leading to the autophagic clearance of cytosolic *Salmonella*. Conversely, optineurin mutants lacking ubiquitin or LC3 binding domains, as well as silencing of optineurin or TBK1, impaired *Salmonella* autophagy and increased intracellular bacterial proliferation. The findings suggest that phosphorylation of autophagy receptors may be a general mechanism for regulating cargo-selective autophagy. The study also highlights the importance of OPTN in innate immunity against cytosolic bacteria by linking the TBK1 signaling pathway to autophagic elimination of pathogens.The study investigates the role of phosphorylation of the autophagy receptor optineurin (OPTN) in the selective autophagy of *Salmonella enterica*. Phosphorylation of OPTN by the protein kinase TANK binding kinase 1 (TBK1) on serine-177 enhances its binding affinity to LC3, leading to the autophagic clearance of cytosolic *Salmonella*. Conversely, optineurin mutants lacking ubiquitin or LC3 binding domains, as well as silencing of optineurin or TBK1, impaired *Salmonella* autophagy and increased intracellular bacterial proliferation. The findings suggest that phosphorylation of autophagy receptors may be a general mechanism for regulating cargo-selective autophagy. The study also highlights the importance of OPTN in innate immunity against cytosolic bacteria by linking the TBK1 signaling pathway to autophagic elimination of pathogens.