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 29-MAY-2013, entry version 57.
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
RT metagenome: complete genome sequence of a macrolide-resistant serotype
RT 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
CC CD46. Also binds to the factor H and factor H-like protein 1.
CC These interactions could contribute to the fact that the M6
CC protein protects the bacterium from the phagocytosis by regulating
CC the complement activation on the bacterial surface (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor
CC (Potential).
CC -!- SIMILARITY: Belongs to the M protein family.
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DR EMBL; CP000003; AAT87854.1; -; Genomic_DNA.
DR RefSeq; YP_061037.1; NC_006086.1.
DR ProteinModelPortal; Q5X9Q9; -.
DR STRING; 286636.M6_Spy1719; -.
DR EnsemblBacteria; AAT87854; AAT87854; M6_Spy1719.
DR GeneID; 2940887; -.
DR KEGG; spa:M6_Spy1719; -.
DR PATRIC; 19725728; VBIStrPyo30273_1787.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000235596; -.
DR OMA; NEKKRTK; -.
DR BioCyc; SPYO286636:GHNO-1800-MONOMER; -.
DR GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR InterPro; IPR005877; Gpos_YSIRK.
DR InterPro; IPR019948; Gram-positive_anchor.
DR InterPro; IPR019950; Gram_pos_anchor.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PRINTS; PR00015; GPOSANCHOR.
DR TIGRFAMs; TIGR01167; LPXTG_anchor; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall; Coiled coil; Complete proteome; Peptidoglycan-anchor;
KW Phagocytosis; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1 42 Potential.
FT CHAIN 43 384 M protein, serotype 6.
FT /FTId=PRO_0000005617.
FT PROPEP 385 415 Removed by sortase (Potential).
FT /FTId=PRO_0000005618.
FT REPEAT 69 75 1.
FT REPEAT 76 82 2.
FT REPEAT 83 89 3.
FT REPEAT 90 96 4; approximate.
FT REPEAT 97 103 5.
FT REGION 69 103 5 X 7 AA approximate tandem repeats of
FT [KMNR]-L-[TQ]-[TDA]-[ENQ]-N-[NDK].
FT REGION 211 279 Binding to CD46 (By similarity).
FT REGION 211 279 Two directly repeated 27 amino acid
FT blocks separated by 15 amino acids.
FT REGION 280 343 Hydrophilic.
FT COILED 54 133 Potential.
FT COILED 170 340 Potential.
FT MOTIF 381 385 LPXTG sorting signal (Potential).
FT COMPBIAS 344 380 Gly/Pro-rich.
FT MOD_RES 384 384 Pentaglycyl murein peptidoglycan amidated
FT threonine (Potential).
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
//