Editing Protein targeting (section)

===Gram-positive bacteria===
{{main|Secretion#Secretion_in_Gram_positive_bacteria|l1=Gram-Positive Bacterial Secretion}}
In most gram-positive bacteria, certain proteins are targeted for export across the plasma membrane and subsequent covalent attachment to the bacterial cell wall. A specialized enzyme, [[sortase]], cleaves the target protein at a characteristic recognition site near the protein C-terminus, such as an LPXTG motif (where X can be any amino acid), then transfers the protein onto the cell wall. Several analogous systems are found that likewise feature a signature motif on the extra-cytoplasmic face, a C-terminal transmembrane domain, and cluster of basic residues on the cytosolic face at the protein's extreme C-terminus. The PEP-CTERM/[[exosortase]] system, found in many Gram-negative bacteria, seems to be related to [[extracellular polymeric substance]] production. The PGF-CTERM/archaeosortase A system in [[archaea]] is related to [[S-layer]] production. The GlyGly-CTERM/rhombosortase system, found in the Shewanella, Vibrio, and a few other genera, seems involved in the release of proteases, nucleases, and other enzymes.