Human plasminogen (hPg) is a single chain multi-modular zymogen containing five kringle domains (K1-K5), four of which interact with lysine. This characteristic is utilized by hPg and its activated product, plasmin (hPm), to interact with receptors containing COOH-terminal lysine residues or through-space isosteric pseudo-lysine residues. In the case of Gram-positive bacteria, Streptococcus pyogenes (GAS), hPg/hPm receptors are primarily focused around the multicopy surface-resident M-protein that is used to characterize the GAS substrain, or other surface proteins, such as the homooctameric glycolytic enzyme enolase (SEn). SEn has no features that suggest the mechanism of its transport from its normal location in the cytoplasm to the cell surface, but we find herein that SEn is translocated to the cell surface by lipid microvesicles (MV) most likely originating from the cytosolic membrane. Through the use of cryogenic-electron microscopy, we provide a high-resolution (