ID   MRP4_STRPY              Reviewed;         388 AA.
AC   P30141;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Fibrinogen- and Ig-binding protein;
DE   AltName: Full=MRP protein;
DE   Flags: Precursor;
GN   Name=mrp4;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AP4 / Serotype M4;
RX   PubMed=1588817; DOI=10.1111/j.1365-2958.1992.tb01557.x;
RA   Stenberg L., O'Toole P., Lindahl G.;
RT   "Many group A streptococcal strains express two different immunoglobulin-
RT   binding proteins, encoded by closely linked genes: characterization of the
RT   proteins expressed by four strains of different M-type.";
RL   Mol. Microbiol. 6:1185-1194(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AP4 / Serotype M4;
RX   PubMed=1528877; DOI=10.1073/pnas.89.18.8661;
RA   O'Toole P., Stenberg L., Rissler M., Lindahl G.;
RT   "Two major classes in the M protein family in group A streptococci.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8661-8665(1992).
CC   -!- FUNCTION: Binds IgG molecules of the Ig1, Ig2 and Ig4 subclasses, and
CC       also binds fibrinogen.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
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DR   EMBL; M87831; AAA26930.1; -; Genomic_DNA.
DR   AlphaFoldDB; P30141; -.
DR   SMR; P30141; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR019950; M_anchor.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   PRINTS; PR00015; GPOSANCHOR.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall; IgG-binding protein; Peptidoglycan-anchor; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..41
FT   CHAIN           42..357
FT                   /note="Fibrinogen- and Ig-binding protein"
FT                   /id="PRO_0000005631"
FT   PROPEP          358..388
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005632"
FT   REGION          308..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           354..358
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        330..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         357
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   388 AA;  42245 MW;  3AB19E8B6CEDA722 CRC64;
     MSKTNPNKLY SLRKLKTGTA SVAVDLTVLG TGLANTTDVK AESRRYQAPP RVLLQGKEAN
     KVFEERKALE KQARDLGDTI NHMSQTISEQ SRKIAALKSE AELKNQQALE ALNNKNKQIS
     DLTNENAQLK EAIEGYVQTI QNASREIAAK QQELAAAKSQ LEAKNAEIEA LKQQDASKTE
     EIAKLQSEAA TLENLLGSAK RELTELQAKL DTATAEKAKL ESQVTTLENL LGSAKRELTD
     LQAKLDAANA EKEKLQSQAA TLEKQLEATK KELADLQAKL AATNQEKEKL EAEAKALKEQ
     LAKQAEELAK LKADKASGAQ KPDTKPGNKE VPTRPSQTRT NTNKAPMAQT KRQLPSTGEE
     TTNPFFTAAA LTVIASAGVL ALKRKEEN