Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the exosortase and its substrate, which is then transferred and covalently attached to the cell membrane (By similarity). This sortase may recognize a tripartite structure consisting of a conserved Pro-Glu-Pro (PEP) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). Disruption of the gene does not significantly alter exopolysaccharide (EPS) production. Belongs to the exosortase/archaeosortase family. Exosortase EpsH subfamily.