ID   M6A_STRP6               Reviewed;         415 AA.
AC   Q5X9Q9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=M protein, serotype 6;
DE   Flags: Precursor;
GN   Name=emm6; OrderedLocusNames=M6_Spy1719;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
CC   -!- FUNCTION: Mediates the attachment of S.pyogenes to skin epithelial
CC       cells through the binding of the human membrane cofactor protein CD46.
CC       Also binds to the factor H and factor H-like protein 1. These
CC       interactions could contribute to the fact that the M6 protein protects
CC       the bacterium from the phagocytosis by regulating the complement
CC       activation on the bacterial surface (By similarity). {ECO:0000250}.
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}.
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DR   EMBL; CP000003; AAT87854.1; -; Genomic_DNA.
DR   RefSeq; WP_011185015.1; NC_006086.1.
DR   AlphaFoldDB; Q5X9Q9; -.
DR   SMR; Q5X9Q9; -.
DR   EnsemblBacteria; AAT87854; AAT87854; M6_Spy1719.
DR   KEGG; spa:M6_Spy1719; -.
DR   HOGENOM; CLU_033717_0_0_9; -.
DR   OMA; MARKDTN; -.
DR   Proteomes; UP000001167; Chromosome.
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   3: Inferred from homology;
KW   Cell wall; Coiled coil; Peptidoglycan-anchor; Phagocytosis; Repeat;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..384
FT                   /note="M protein, serotype 6"
FT                   /id="PRO_0000005617"
FT   PROPEP          385..415
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005618"
FT   REPEAT          69..75
FT                   /note="1"
FT   REPEAT          76..82
FT                   /note="2"
FT   REPEAT          83..89
FT                   /note="3"
FT   REPEAT          90..96
FT                   /note="4; approximate"
FT   REPEAT          97..103
FT                   /note="5"
FT   REGION          69..103
FT                   /note="5 X 7 AA approximate tandem repeats of [KMNR]-L-
FT                   [TQ]-[TDA]-[ENQ]-N-[NDK]"
FT   REGION          75..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..279
FT                   /note="Binding to CD46"
FT                   /evidence="ECO:0000250"
FT   REGION          211..279
FT                   /note="Two directly repeated 27 amino acid blocks separated
FT                   by 15 amino acids"
FT   REGION          247..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..343
FT                   /note="Hydrophilic"
FT   REGION          332..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          54..133
FT                   /evidence="ECO:0000255"
FT   COILED          170..340
FT                   /evidence="ECO:0000255"
FT   MOTIF           381..385
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        82..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         384
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   415 AA;  45751 MW;  4DA7A7451C04A699 CRC64;
     MAKNNTNRHY SLRKLKKGTA SVAVALSVIG AGLVVNTNEV SARVFPRGTV ENPDKARELL
     NKYDVENSML QANNDKLTTE NKNLTDQNKE LKAEENRLTT ENKGLTKKLS EAEEEAANKE
     QESKETIGTL KKILDETVKD KIAREQKSKQ DIGALKQELA KKDEGNKVSE ASRKGLRRDL
     DASREAKKQV EKDLANLTAE LDKVKEEKQI SDASRKGLRR DLDASREAKK QVEKDLANLT
     AELDKVKEEK QISDASRQGL RRDLDASREA KKQVEKALEE ANSKLAALEK LNKELEESKK
     LTEKEKAELQ AKLEAEAKAL KEQLAKQAEE LAKLRAGKAS DSQTPDAKPG NKVVPGKGQA
     PQAGTKPNQN KAPMKETKRQ LPSTGETANP FFTAAALTVM ATAGVAAVVK RKEEN