Protein adsorption and assembly at interfaces provide a potentially versatile route to create useful constructs for fluid compartmentalization. In this context, we consider the interfacial assembly of a bacterial biofihn protein, Bs1A, at air-water and oil-water interfaces. Densely packed, high modulus monolayers form at air-water interfaces, leading to the formation of flattened sessile water drops. BslA forms elastic sheets at oil water interfaces, leading to the production of stable monodisperse oil-in-water microcapsules. By contrast, water-in-oil microcapsules are unstable but display arrested rather than full coalescence on contact. The disparity in stability likely originates from a low areal density of BslA hydrophobic caps on the exterior surface of water-in-oil micro capsules, relative to the inverse case. In direct analogy with small molecule surfactants, the lack of stability of individual water-in-oil microcapsules is consistent with the large value of the hydrophilic-lipophilic balance (HLB number) calculated based on the BslA crystal structure. The occurrence of arrested coalescence indicates that the surface activity of BsIA is similar to that of colloidal particles that produce Pickering emulsions, with the stability of partially coalesced structures ensured by interfacial jamming. Micropipette aspiration and flow in tapered capillaries experiments reveal intriguing reversible and nonreversible modes of mechanical deformation, respectively. The mechanical robustness of the microcapsules and the ability to engineer their shape and to design highly specific binding responses through protein engineering suggest that these microcapsules may be useful for biomedical applications.