M22_STRPY
ID M22_STRPY Reviewed; 372 AA.
AC P50469;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=M protein, serotype 2.2;
DE Flags: Precursor;
GN Name=emmL2.2;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T2/44/RB4/119;
RX PubMed=1370269; DOI=10.1128/iai.60.1.124-135.1992;
RA Bessen D.E., Fischetti V.A.;
RT "Nucleotide sequences of two adjacent M or M-like protein genes of group A
RT streptococci: different RNA transcript levels and identification of a
RT unique immunoglobulin A-binding protein.";
RL Infect. Immun. 60:124-135(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fischetti V.A., Bessen D.E.;
RT "Immunoglobulin A binding protein.";
RL Patent number US5556944, 17-SEP-1996.
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}.
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DR EMBL; X61276; CAA43582.1; -; Genomic_DNA.
DR EMBL; I26204; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; S23326; S23326.
DR AlphaFoldDB; P50469; -.
DR SMR; P50469; -.
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; IPR003345; M_repeat.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02370; M; 3.
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..41
FT /evidence="ECO:0000255"
FT CHAIN 42..342
FT /note="M protein, serotype 2.2"
FT /id="PRO_0000005613"
FT PROPEP 343..372
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005614"
FT REPEAT 131..153
FT /note="C-1"
FT REPEAT 173..195
FT /note="C-2"
FT REPEAT 222..244
FT /note="C-3"
FT REGION 125..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..244
FT /note="3 X repeats, type C"
FT REGION 211..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 339..343
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 125..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 342
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 372 AA; 41149 MW; E8FD5D0920C95C74 CRC64;
MARQQTKKNY SLRKLKTGTA SVAVALTVLG AGFANQTEVR ADEAKKMEVK ESEKESQYKT
LALRGENADL RNVNAKYLEK INAEEEKNKK LEAINKELNE NYYKLQDGID ALEKEKEDLK
TTLAKTTKEN EISEASRKGL SRDLEASRTA KKELEAKHQK LEAENKKLTE GNQVSEASRK
GLSNDLEASR AAKKELEAKY QKLETDHQAL EAKHQKLEAD YQVSETSRKG LSRDLEASRE
ANKKVTSELT QAKAQLSALE ESKKLSEKEK AELQAKLDAQ GKALKEQLAK QTEELAKLRA
EKAAGSKTPA TKPANKERSG RAAQTATRPS QNKGMRSQLP STGEAANPFF TAAAATVMVS
AGMLALKRKE EN