ID   MAP_STAAU               Reviewed;         689 AA.
AC   Q53599;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Protein map;
DE   AltName: Full=MHC class II analog protein;
DE   Flags: Precursor;
GN   Name=map;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-40.
RC   STRAIN=FDA 574;
RX   PubMed=7545162; DOI=10.1074/jbc.270.37.21457;
RA   Joensson K., McDevitt D., McGavin M.H., Patti J.M., Hoeoek M.;
RT   "Staphylococcus aureus expresses a major histocompatibility complex class
RT   II analog.";
RL   J. Biol. Chem. 270:21457-21460(1995).
RN   [2]
RP   FUNCTION.
RX   PubMed=12438444; DOI=10.1172/jci16318;
RA   Lee L.Y., Miyamoto Y.J., McIntyre B.W., Hook M., McCrea K.W., McDevitt D.,
RA   Brown E.L.;
RT   "The Staphylococcus aureus Map protein is an immunomodulator that
RT   interferes with T cell-mediated responses.";
RL   J. Clin. Invest. 110:1461-1471(2002).
CC   -!- FUNCTION: Both native and recombinant protein bound to labeled
CC       vitronectin, fibrinogen, recombinant osteopontin and fibronectin. It
CC       was also shown to be able to bind to a 15-amino acid synthetic peptide
CC       of vitronectin. Map could affect the severity of arthritis and
CC       osteomyelitis in mice through a T-cell-mediated mechanism and could
CC       play a role in abscess formation through a T-cell-independent
CC       mechanisms. It could potentiate the survival of the bacterium by
CC       modulating host immunity. {ECO:0000269|PubMed:12438444}.
CC   -!- DOMAIN: Each MAP domain contains a 31-residue subdomain that shares
CC       striking sequence homology with a segment present in the peptide
CC       binding groove of the beta chain of the MHC class II proteins from
CC       different mammalian species.
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DR   EMBL; U20503; AAC43470.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53599; -.
DR   SMR; Q53599; -.
DR   MEROPS; I96.001; -.
DR   InterPro; IPR005298; MAP_dom.
DR   Pfam; PF03642; MAP; 6.
DR   PROSITE; PS51223; MAP; 6.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:7545162"
FT   CHAIN           31..689
FT                   /note="Protein map"
FT                   /id="PRO_0000021641"
FT   REPEAT          45..154
FT                   /note="MAP 1"
FT   REPEAT          155..264
FT                   /note="MAP 2"
FT   REPEAT          265..374
FT                   /note="MAP 3"
FT   REPEAT          375..474
FT                   /note="MAP 4"
FT   REPEAT          475..584
FT                   /note="MAP 5"
FT   REPEAT          589..689
FT                   /note="MAP 6"
SQ   SEQUENCE   689 AA;  77049 MW;  92EA0A0B8E647C69 CRC64;
     MKFKSLITTT LALGVIASTG ANLDTNEASA AAKQIDKSSS SLHHGYSKIQ IPYTITVNGT
     SQNILSSLTF NKNQQISYKD IENKVKSVLY FNRGISDIDL RLSKQAKYTV HFKNGTKRVV
     DLKAGIHTAD LINTSDIKAI SVNVDTKKQV KDKEAKANVQ VPYTITVNGT SQNILSNLTF
     KKNQQISYKD LENNVKSVLK SNRGITDVDL RLSKQAKFTV NFKNGTKKVI DLKAGIYTAN
     LINTGGIKNI NINVETKKQA KDKEAKVNNQ VPYSINLNGT TTNIQSNLAF SNKPWTNYKN
     LTTKVKSVLK SDRGVSERDL KHAKKAYYTV YFKNGGKRVI HLNSNIYTAN LVHAKDVKRI
     EVTVKTVSKV KAERYVPYTI AVNGASNPTL SDLKFTGDSR VSYSDIKKKV KSVLKHDRGI
     GERELKYAEK ATYTVHFKNG TKKVINLNSN ISQLNLLYVK DIKNIDIDVK TGAKAKVYSY
     VPYTIAVNGT TTPIASKLKL SNKQLIGYQD LNKKVKSVLK HDRGINDIEL KFAKQAKYTI
     HFKNGKTQVV DLKSDIFTRN LFSVKDIKKI DINVKQQSKS NKALNKVTNK ATKVKFPVTI
     NGFSNLVSNE FAFLHPHKIT TNDLNAKLRL ALRSDQGITK HDIGLSERTV YKVYFKDGSS
     KLEDLKAAKQ DSKVFKATDI KKVDIEIKF