M49_STRP9
ID M49_STRP9 Reviewed; 389 AA.
AC P16947; P97165;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=M protein, serotype 49;
DE Flags: Precursor;
GN Name=emm49;
OS Streptococcus pyogenes serotype M49.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301452;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687231; DOI=10.1128/jb.171.12.6397-6408.1989;
RA Haanes E.J., Cleary P.P.;
RT "Identification of a divergent M protein gene and an M protein-related gene
RT family in Streptococcus pyogenes serotype 49.";
RL J. Bacteriol. 171:6397-6408(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RC STRAIN=CS101 / Serotype M49;
RX PubMed=1385809; DOI=10.1128/jb.174.15.4967-4976.1992;
RA Haanes E.J., Heath D.G., Cleary P.P.;
RT "Architecture of the vir regulons of group streptococci parallels opacity
RT factor phenotype and M protein class.";
RL J. Bacteriol. 174:4967-4976(1992).
RN [3]
RP PROTEIN SEQUENCE OF 42-188.
RC STRAIN=B915 / Serotype M49;
RX PubMed=2451662; DOI=10.1016/s0021-9258(18)60681-7;
RA Khandke K.M., Fairwell T., Acharya A.S., Trus B.L., Manjula B.N.;
RT "Complete amino acid sequence of streptococcal PepM49 protein, a nephritis-
RT associated serotype. Conserved conformational design among sequentially
RT distinct M protein serotypes.";
RL J. Biol. Chem. 263:5075-5082(1988).
RN [4]
RP PROTEIN SEQUENCE OF 46-105.
RC STRAIN=B915 / Serotype M49;
RX PubMed=3298523; DOI=10.1084/jem.166.1.151;
RA Khandke K.M., Fairwell T., Manjula B.N.;
RT "Difference in the structural features of streptococcal M proteins from
RT nephritogenic and rheumatogenic serotypes.";
RL J. Exp. Med. 166:151-162(1987).
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 -!- SUBUNIT: Homodimer. {ECO:0000305}.
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; M23689; AAA26918.1; -; Genomic_DNA.
DR EMBL; M31789; AAA26868.1; -; Genomic_DNA.
DR EMBL; M86806; AAA26888.1; -; Genomic_DNA.
DR PIR; A43715; A43715.
DR PDB; 5HZP; X-ray; 2.74 A; A/C=42-127.
DR PDBsum; 5HZP; -.
DR AlphaFoldDB; P16947; -.
DR SMR; P16947; -.
DR PHI-base; PHI:6880; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Coiled coil; Direct protein sequencing;
KW Peptidoglycan-anchor; Phagocytosis; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..41
FT /evidence="ECO:0000269|PubMed:2451662"
FT CHAIN 42..359
FT /note="M protein, serotype 49"
FT /id="PRO_0000005625"
FT PROPEP 360..389
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005626"
FT REPEAT 89..99
FT /note="A-1"
FT REPEAT 125..135
FT /note="A-2"
FT REPEAT 159..200
FT /note="B-1"
FT REPEAT 201..242
FT /note="B-2"
FT REPEAT 243..273
FT /note="B-3; truncated"
FT REGION 89..135
FT /note="2 X repeats, type A"
FT REGION 93..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..273
FT /note="3 X tandem repeats, type B"
FT REGION 194..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 356..360
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 93..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 359
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 42
FT /note="A -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="A -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..52
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="V -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5HZP"
FT HELIX 61..113
FT /evidence="ECO:0007829|PDB:5HZP"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5HZP"
SQ SEQUENCE 389 AA; 43915 MW; A52579C03FEFBACE CRC64;
MARKDTNKQY SLRKLKTGTA SVAVAVAVLG AGFANQTEVK AAEKKVEAKV EVAENNVSSV
ARREKELYDQ IADLTDKNGE YLERIGELEE RQKNLEKLEH QSQVAADKHY QEQAKKHQEY
KQEQEERQKN QEQLERKYQR EVEKRYQEQL QKQQQLETEK QISEASRKSL SRDLEASREA
KKKVEADLAA LTAEHQKLKE EKQISDASRQ GLSRDLEASR EAKKKVEADL AALTAEHQKL
KEEKQISDAS RQGLSRDLEA SREAKKKVEA DLAEANSKLQ ALEKLNKELE EGKKLSEKEK
AELQARLEAE AKALKEQLAK QAEELAKLKG NQTPNAKVAP QANRSRSAMT QQKRTLPSTG
ETANPFFTAA AATVMVSAGM LALKRKEEN
