| Description | Surface proteins from Gram-positive cocci are covalently linked to the bacterial cell wall by sortase, a membrane-anchored transpeptidase that cleaves proteins between the threonine and the glycine of a conserved LPxTG motif, with the formation of a thioester between the conserved cysteine of sortase and the threonine carboxyl group. The newly liberated C terminus of the threonine is transferred via an amide bond exchange to the amino group of the pentaglycine wall crossbridge, thereby tethering the C terminus end of the surface protein to the bacterial peptidoglycan [, ].Surface proteins from Gram-positive cocci contain an N-terminal signal peptide and a C-terminal sorting signal. The 35-residue sorting signal is composed of a conserved LPxTG motif, a hydrophobic domain, and a tail of positively charged residues.In the case of immunoglobulin A1 proteases, the typical Gram-positive cell wall anchor motif LPxTG is located in their N-terminal regions, in contrast with other known streptococcal and staphylococcal proteins [].This entry represents a domain covering the LPxTG motif, the hydrophobic stretch and the positively charged region. | Name | LPXTG cell wall anchor domain |
| Short Name | LPXTG_anchor | Type | Domain |
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