M6B_STRPY
ID M6B_STRPY Reviewed; 483 AA.
AC P08089;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=M protein, serotype 6;
DE Flags: Precursor;
GN Name=emm6;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3511046; DOI=10.1016/s0021-9258(17)35993-8;
RA Hollingshead S.K., Fischetti V.F., Scott J.R.;
RT "Complete nucleotide sequence of type 6 M protein of the group A
RT Streptococcus. Repetitive structure and membrane anchor.";
RL J. Biol. Chem. 261:1677-1686(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-122.
RX PubMed=3885219; DOI=10.1073/pnas.82.6.1822;
RA Scott J.R., Pulliam W.M., Hollingshead S.K., Fischetti V.A.;
RT "Relationship of M protein genes in group A streptococci.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1822-1826(1985).
RN [3]
RP INTERACTION WITH HUMAN CD46.
RC STRAIN=JRS4 / Serotype M6;
RX PubMed=7708671; DOI=10.1073/pnas.92.7.2489;
RA Okada N., Liszewski M.K., Atkinson J.P., Caparon M.;
RT "Membrane cofactor protein (CD46) is a keratinocyte receptor for the M
RT protein of the group A streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2489-2493(1995).
RN [4]
RP INTERACTION WITH HUMAN CD46.
RC STRAIN=JRS4 / Serotype M6;
RX PubMed=11971006; DOI=10.4049/jimmunol.168.9.4585;
RA Giannakis E., Jokiranta T.S., Ormsby R.J., Duthy T.G., Male D.A.,
RA Christiansen D., Fischetti V.A., Bagley C., Loveland B.E., Gordon D.L.;
RT "Identification of the streptococcal M protein binding site on membrane
RT cofactor protein (CD46).";
RL J. Immunol. 168:4585-4592(2002).
RN [5]
RP INTERACTION WITH HUMAN FACTOR H.
RX PubMed=7806351; DOI=10.1128/iai.63.1.149-153.1995;
RA Fischetti V.A., Horstmann R.D., Pancholi V.;
RT "Location of the complement factor H binding site on streptococcal M6
RT protein.";
RL Infect. Immun. 63:149-153(1995).
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.
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; M11338; AAA26920.1; -; Genomic_DNA.
DR PIR; A26297; A26297.
DR RefSeq; WP_047149520.1; NZ_CP011415.1.
DR AlphaFoldDB; P08089; -.
DR SMR; P08089; -.
DR PRIDE; P08089; -.
DR PATRIC; fig|1314.199.peg.1662; -.
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; Peptidoglycan-anchor; Phagocytosis; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..42
FT CHAIN 43..452
FT /note="M protein, serotype 6"
FT /id="PRO_0000005619"
FT PROPEP 453..483
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005620"
FT REPEAT 69..75
FT /note="1-1"
FT REPEAT 76..82
FT /note="2-1"
FT REPEAT 83..89
FT /note="3-1"
FT REPEAT 90..96
FT /note="4-1"
FT REPEAT 97..103
FT /note="5-1"
FT REPEAT 104..110
FT /note="6-1"
FT REPEAT 111..117
FT /note="7-1"
FT REPEAT 118..124
FT /note="8-1"
FT REPEAT 125..131
FT /note="9-1; approximate"
FT REPEAT 132..138
FT /note="10-1"
FT REPEAT 157..181
FT /note="1-2"
FT REPEAT 182..206
FT /note="2-2"
FT REPEAT 207..231
FT /note="3-2"
FT REPEAT 232..256
FT /note="4-2"
FT REPEAT 257..281
FT /note="5-2; approximate"
FT REGION 69..138
FT /note="10 X 7 AA approximate tandem repeats of [KMNR]-L-
FT [TQ]-[TDA]-[ENQ]-N-[NDK]"
FT REGION 74..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..269
FT /note="4.5 X 25 AA tandem repeats of E-[NS]-K-E-[TA]-I-G-T-
FT L-K-K-[TI]-L-D-E-T-V-K-D-K-I-A-[KR]-E-Q"
FT REGION 255..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..347
FT /note="Binding to CD46"
FT REGION 279..347
FT /note="Two directly repeated 27 amino acid blocks separated
FT by 15 amino acids"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..411
FT /note="Hydrophilic"
FT REGION 400..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..171
FT /evidence="ECO:0000255"
FT COILED 280..408
FT /evidence="ECO:0000255"
FT MOTIF 449..453
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 74..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 452
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 483 AA; 53472 MW; 68F87F28DB53A448 CRC64;
MAKNNTNRHY SLRKLKKGTA SVAVALSVIG AGLVVNTNEV SARVFPRGTV ENPDKARELL
NKYDVENSML QANNDKLTTE NNNLTDQNKN LTTENKNLTD QNKNLTTENK NLTDQNKNLT
TENKELKAEE NRLTTENKGL TKKLSEAEEE AANKERENKE AIGTLKKTLD ETVKDKIAKE
QESKETIGTL KKTLDETVKD KIAKEQESKE TIGTLKKTLD ETVKDKIAKE QESKETIGTL
KKILDETVKD KIAREQKSKQ DIGALKQELA KKDEGNKVSE ASRKGLRRDL DASREAKKQV
EKDLANLTAE LDKVKEEKQI SDASRQGLRR DLDASREAKK QVEKALEEAN SKLAALEKLN
KELEESKKLT EKEKAELQAK LEAEAKALKE QLAKQAEELA KLRAGKASDS QTPDAKPGNK
VVPGKGQAPQ AGTKPNQNKA PMKETKRQLP STGETANPFF TAAALTVMAT AGVAAVVKRK
EEN
