The proper synthesis and maintenance of a cell envelope is essential for bacterial fitness. Environmental stresses such as cell envelope targeting antibiotics require bacteria to mount protective cell envelope stress responses to maintain the integrity of the cell envelope. In this dissertation I discuss two independent studies detailing the identification of two novel cell envelope stress responses in Bacillus subtilis. In B. subtilis, the synthesis and regulation of the cell wall and the cell membrane in response to extracellular stresses has been extensively investigated. However, if and how the synthesis of these structures is coordinated remains unclear. Here, I investigate how a reduction in fatty acid synthesis (FAS) can compensate for limitations in peptidoglycan (PG) synthesis. Synthesis of a cell wall is mediated by the elongasome complex acting in concert with the class A PBPs (aPBPs). Loss of aPBP activity in conjunction with an inability to properly upregulate the elongasome yields a synthetically lethal PG-limited cell. This study uses PG-limited cells as a model system to uncover novel suppressor mutations that restore viability. One suppressor mutation identified is an altered function transcriptional repressor, FapR*, that acts as a super-repressor to decrease the transcription of FAS genes. Limitations in fatty acidsynthesis caused by either FapR* or cerulenin, a FAS inhibiting antibiotic, rescue PG-limited cells and can aid in β-lactam resistance. This study suggests that limitations in PG synthesis create an imbalance between the synthesis of PG and cell membrane, and that B. subtilis lacks a robust mechanism to reduce membrane synthesis in response to limitations in PG synthesis. Secondly, this study identifies YtpA as a member of the B. subtilis intrinsic cell envelope stress response. I find that induction of YtpA, a membrane associated protein, increases membrane fluidity. Further, I show that in B. subtilis strains genetically sensitized to bacitracin, deletion of ytpA further exacerbates bacitracin sensitivity. Membrane modifications may impact the essential recycling of bactoprenol, the target of bacitracin, across the membrane. This suggests that YtpA modifies the membrane to support bactoprenol recycling and is a minor member of the bacitracin stress response.