ID   M12_STRPY               Reviewed;         564 AA.
AC   P19401; Q6LCZ1;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=M protein, serotype 12;
DE   Flags: Precursor; Fragment;
GN   Name=emm12;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CS24 / Serotype M12;
RX   PubMed=2445730; DOI=10.1128/jb.169.12.5633-5640.1987;
RA   Robbins J.C., Spanier J.G., Jones S.J., Simpson W.J., Cleary P.P.;
RT   "Streptococcus pyogenes type 12 M protein gene regulation by upstream
RT   sequences.";
RL   J. Bacteriol. 169:5633-5640(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-111.
RX   PubMed=7891551; DOI=10.1111/j.1365-2958.1994.tb01301.x;
RA   Whatmore A.M., Kapur V., Sullivan D.J., Musser J.M., Kehoe M.A.;
RT   "Non-congruent relationships between variation in emm gene sequences and
RT   the population genetic structure of group A streptococci.";
RL   Mol. Microbiol. 14:619-631(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-54.
RX   PubMed=2473037; DOI=10.1128/iai.57.8.2457-2461.1989;
RA   Kraus W., Seyer J.M., Beachey E.H.;
RT   "Vimentin-cross-reactive epitope of type 12 streptococcal M protein.";
RL   Infect. Immun. 57:2457-2461(1989).
CC   -!- FUNCTION: This protein is one of the different antigenic serotypes of
CC       protein M. Protein M is closely associated with virulence of the
CC       bacterium and can render the organism resistant to phagocytosis.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- SIMILARITY: Belongs to the M protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M18269; AAA88573.1; -; Genomic_DNA.
DR   EMBL; U11937; AAA99553.1; -; Genomic_DNA.
DR   PIR; A40174; A60115.
DR   AlphaFoldDB; P19401; -.
DR   SMR; P19401; -.
DR   PRIDE; P19401; -.
DR   eggNOG; COG1196; Bacteria.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; 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   Pfam; PF04650; YSIRK_signal; 1.
DR   PRINTS; PR00015; GPOSANCHOR.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Coiled coil; Direct protein sequencing; Peptidoglycan-anchor;
KW   Phagocytosis; Repeat; Secreted; Signal; Virulence.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000269|PubMed:2473037"
FT   CHAIN           42..545
FT                   /note="M protein, serotype 12"
FT                   /id="PRO_0000005621"
FT   PROPEP          546..>564
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005622"
FT   REGION          372..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          44..505
FT                   /evidence="ECO:0000255"
FT   MOTIF           542..546
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        523..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         545
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   NON_TER         564
SQ   SEQUENCE   564 AA;  62904 MW;  5F1549DACAA77B46 CRC64;
     MAKNTTNRHY SLRKLKTGTA SVAVALTVVG AGLVAGQTVR ADHSDLVAEK QRLEDLGQKF
     ERLKQRSELY LQQYYDNKSN GYKGDWYVQQ LKMLNRDLEQ AYNELSGEAH KDALGKLGID
     NADLKAKITE LEKSVEEKND VLSQIKKELE EAEKDIQFGR EVHAADLLRH KQEIAEKENV
     ISKLNGELQP LKQKVDETDR NLQQEKQKVL SLEQQLAVTK ENAKKDFELA ALGHQLADKE
     YNAKIAELES KLADAKKDFE LAALGHQHAH NEYQAKLAEK DGQIKQLEEQ KQILDASRKG
     TARDLEAVRQ AKKATEAELN NLKAELAKVT EQKQILDASR KGTARDLEAV RKSKKQQVEA
     ALKQLEEQNK ISEASRKGLR RDLDTSREAK KQVEKDLANL TAELDKVKEE KQISDASRQG
     LRRDLDASRE AKKQVEKALE EANSKLAALE KLNKDLEESK KLTEKEKAEL QAKLEAEAKA
     LKEQLAKQAE ELAKLRAGKA SDSQTPDAKP GNKAVPGKGQ APQAGTKPNQ NKAPMKETKR
     QLPSTGETAN PFFTAAALTV MAAA