{PDOC51780}
{PS51780; GW}
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* GW domain profile *
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The GW  domain  or cell wall targeting (CWT) signal is a module of about 80-90
amino acids named for a conserved Gly-Trp (GW) dipeptide. GW domains have only
been identified  in  Gram-positive  bacteria  and form a small protein family.
They are  divergent  members  of the SH3 family (see <PDOC50002>). However, GW
domains are  unlikely  to  mimic  SH3 domains functionally, as their potential
peptide-binding sites  are  destroyed  or blocked. GW domains may constitute a
motif for  cell-surface anchoring in Listeria and other Gram-positive bacteria
[1,2].

The GW  domain  is composed of seven beta-strands, five of which are organized
into an  open  barrel  conformation like that of SH3 domains (see <PDB:1M9S>).
The eponymous  GW  dipeptide,  located  in  the  fourth  beta-strand,  is more
conserved in  GW  domains than in SH3 domains. Both the glycine and tryptophan
are buried  in  GW proteins, while the equivalent residues in SH3 proteins are
surface accesible,  perhaps  explaning the greater conservation in GW proteins
[2,3].

Some proteins known to contain a GW domain are listed below:

 - Listeria  monocytogenes internalin B (InlB), an invasion protein associated
   with the bacterial surface.
 - Listeria  monocytogenes  autolysin,  amidase  (Ami), a surface protein with
   bacteriolytic activity.

The profile we developed covers the entire GW domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2015 / First entry.

[ 1] Braun L., Dramsi S., Dehoux P., Bierne H., Lindahl G., Cossart P.
     "InlB: an invasion protein of Listeria monocytogenes with a novel type
     of surface  association."
     Mol. Microbiol. 25:285-294(1997).
     PubMed=9282740
[ 2] Marino M., Banerjee M., Jonquieres R., Cossart P., Ghosh P.
     "GW domains of the Listeria monocytogenes invasion protein InlB are
     SH3-like and mediate binding to host ligands."
     EMBO J. 21:5623-5634(2002).
     PubMed=12411480
[ 3] Zoll S., Schlag M., Shkumatov A.V., Rautenberg M., Svergun D.I.,
     Goetz F., Stehle T.
     "Ligand-binding properties and conformational dynamics of autolysin
     repeat domains in staphylococcal cell wall recognition."
     J. Bacteriol. 194:3789-3802(2012).
     PubMed=22609916; DOI=10.1128/JB.00331-12

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