{PDOC00373}
{PS50847; GRAM_POS_ANCHORING}
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* Gram-positive cocci surface proteins LPxTG motif profile *
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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 [1,2,3].

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.  This  structure  is  represented in the following schematic
representation:

                                           +-- sorting signal ---+
                                           |                     |
  +------+---------------------------------+-----+-------------+-+
  |Signal|                                 |LPxTG| Hydrophobic |+|
  +------+---------------------------------+-----+-------------+-+

  'Signal': signal peptide;
  'Hydrophobic': hydrophobic domain;
  '+': positive charged tail.

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 [4].

Some proteins  known  to  contain  LPxTG  motif  containing sorting signal are
listed below:

 - Aggregation substance from streptococcus faecalis (asa1).
 - C5a peptidase from Streptococcus pyogenes (scpA).
 - C protein alpha-antigen from Streptococcus agalactiae (bca).
 - Cell surface antigen I/II (PAC) from Streptococcus mutans.
 - Dextranase from Streptococcus downei (dex).
 - Fibronectin-binding protein from Staphylococcus aureus (fnbA).
 - Fimbrial subunits from Actinomyces naeslundii and viscosus.
 - IgA binding protein from Streptococcus pyogenes (arp4).
 - IgA binding protein (B antigen) from Streptococcus agalactiae (bag).
 - IgG binding proteins from Streptococci and Staphylococcus aureus.
 - Internalin A from Listeria monocytogenes (inlA).
 - M proteins from streptococci.
 - Muramidase-released protein from Streptococcus suis (mrp).
 - Nisin leader peptide processing protease from Lactococcus lactis (nisP).
 - Protein A from Staphylococcus aureus.
 - Trypsin-resistant surface T protein from streptococci.
 - Wall-associated protein from Streptococcus mutans (wapA).
 - Wall-associated serine proteinases from Lactococcus lactis.

The profile  we  developed covers the LPxTG motif, the hydrophobic stretch and
the positively charged region.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: This profile replaces a pattern whose specificity was inadequate.

-Last update: July 2018 / Profile revised.

[ 1] Mazmanian S.K., Liu G., Ton-That H., Schneewind O.
     "Staphylococcus aureus sortase, an enzyme that anchors surface
     proteins to the cell wall."
     Science 285:760-763(1999).
     PubMed=10427003
[ 2] Ton-That H., Liu G., Mazmanian S.K., Faull K.F., Schneewind O.
     Proc. Natl. Acad. Sci. U.S.A. 96:12424-12429(1999).
[ 3] Perry A.M., Ton-That H., Mazmanian S.K., Schneewind O.
     "Anchoring of surface proteins to the cell wall of Staphylococcus
     aureus. III. Lipid II is an in vivo peptidoglycan substrate for
     sortase-catalyzed surface protein anchoring."
     J. Biol. Chem. 277:16241-16248(2002).
     PubMed=11856734; DOI=10.1074/jbc.M109194200
[ 4] Poulsen K., Reinholdt J., Jespersgaard C., Boye K., Brown T.A.,
     Hauge M., Kilian M.
     "A comprehensive genetic study of streptococcal immunoglobulin A1
     proteases: evidence for recombination within and between species."
     Infect. Immun. 66:181-190(1998).
     PubMed=9423856

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