{PDOC51223}
{PS51223; MAP}
{BEGIN}
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* MAP repeat profile *
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Map  (MHC  class  II  analogous  protein),  also  known  as eap (extracellular
adherence  protein) and p70, is exclusively found in Staphylococcus aureus. It
is  a cell-wall associated protein, which is capable of binding to a number of
different  extracellular  matrix glycoploteins and plasma proteins, and to the
cell  surface of Staphylococcus aureus. Besides the broad binding specificity,
map  has been shown to be important in the adherence to and internalization of
Staphylococcus  aureus  by  eukaryotic  cells  as  well  as  being  capable of
modulating   inflammatory   response  through  its  interactions  with  ICAM-1
(intercellular  adhesion  molecule-1),  although  its  biological role in vivo
remains to date unclear [1].

The  protein  consists  of  a  signal peptide followed by a unique sequence of
about  20  amino  acids and four to six repeated MAP domains of 110-amino acid
residues.  Within  each  repeat there is a subdomain consisting of 31 residues
that  was  found  to be highly homologous to the N-terminal beta-chain of many
MHC class II molecules [2].

The  crystal  structure of the MAP domain has been solved (see <PDB:1YN3>) and
shows  a core fold that is comprised of an alpha-helix lying diagonally across
a   five-stranded,  mixed  beta-sheet.  This  structure  is  very  similar  to
the C-terminal domain of  bacterial superantigens [3].

The  profile we developed covers the entire MAP repeat.

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

-Note:  MAP  repeats have been found in all but 5 of 140 Staphylococcus aureus
 strains examined, but they were not detected in reference strains or clinical
 isolates of Staphylococcus epidermidis [1].

-Last update: June 2006 / First entry.

[ 1] Harraghy N., Hussain M., Haggar A., Chavakis T., Sinha B.,
     Herrmann M., Flock J.I.
     "The adhesive and immunomodulating properties of the multifunctional
     Staphylococcus aureus protein Eap."
     Microbiology 149:2701-2707(2003).
     PubMed=14523103
[ 2] Jonsson K., McDevitt D., McGavin M.H., Patti J.M., Hook M.
     "Staphylococcus aureus expresses a major histocompatibility complex
     class II analog."
     J. Biol. Chem. 270:21457-21460(1995).
     PubMed=7545162
[ 3] Geisbrecht B.V., Hamaoka B.Y., Perman B., Zemla A., Leahy D.J.
     "The crystal structures of EAP domains from Staphylococcus aureus
     reveal an unexpected homology to bacterial superantigens."
     J. Biol. Chem. 280:17243-17250(2005).
     PubMed=15691839; DOI=10.1074/jbc.M412311200

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