The neuronal G protein-coupled receptor NMUR-1, a homolog to the mammalian neuromedin U receptor, has been implicated in the specificity of Caenorhabditis elegans innate immune response against pathogen infections. NMUR-1 controls C. elegans transcription activity by regulating transcription factors, which, in turn control the expression of distinct defense genes. This study further investigates the role of NMUR-1 at the protein level in regulating innate immune responses against pathogens Salmonella enterica and Enterococcus faecalis by utilizing mass spectrometry-based quantitative proteomics. We found that NMUR-1 regulates a class of proteins responsible for transmembrane transport during infection. Specifically, a group of proteins forming F1FO ATP synthase responsible for ATP biosynthesis is downregulated in NMUR-1 loss of function mutants during both S. enterica and E. faecalis infections. ATP measurements further revealed that nmur-1 mutants have reduced ATP production in response to both S. enterica and E. faecalis infections. Functional assays demonstrated that inhibiting F1FO ATP synthase using RNA interference or chemical modification mimicked the survival phenotypes of the untreated nmur-1 knockout mutants on S. enterica and E. faecalis. These findings provide valuable insights into the mechanism by which NMUR-1 regulates energy homeostasis at the protein level as part of an innate immune response against specific pathogens.