SPEH_STRPY
ID SPEH_STRPY Reviewed; 236 AA.
AC P0C0I6; Q9X5C8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Exotoxin type H;
DE AltName: Full=SPE H;
DE Flags: Precursor;
GN Name=speH;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M15;
RX PubMed=9874566; DOI=10.1084/jem.189.1.89;
RA Proft T., Moffatt S.L., Berkahn C.J., Fraser J.D.;
RT "Identification and characterization of novel superantigens from
RT Streptococcus pyogenes.";
RL J. Exp. Med. 189:89-102(1999).
CC -!- FUNCTION: Mitogenic for human peripheral blood lymphocytes.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Binds to major histocompatibility complex class II beta
CC chain.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; AF124500; AAD30989.1; -; Genomic_DNA.
DR RefSeq; WP_010922229.1; NZ_WVGJ01000001.1.
DR PDB; 1ET9; X-ray; 1.90 A; A=33-236.
DR PDB; 1EU4; X-ray; 2.50 A; A=33-236.
DR PDBsum; 1ET9; -.
DR PDBsum; 1EU4; -.
DR AlphaFoldDB; P0C0I6; -.
DR SMR; P0C0I6; -.
DR PATRIC; fig|1314.197.peg.958; -.
DR OMA; AQEACEC; -.
DR EvolutionaryTrace; P0C0I6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR008992; Enterotoxin.
DR InterPro; IPR006126; Staph/Strept_toxin_CS.
DR InterPro; IPR006173; Staph_tox_OB.
DR InterPro; IPR016091; SuperAg_toxin_C.
DR InterPro; IPR013307; Superantigen_bac.
DR InterPro; IPR006123; Toxin_b-grasp_Staph/Strep.
DR Pfam; PF02876; Stap_Strp_tox_C; 1.
DR Pfam; PF01123; Stap_Strp_toxin; 1.
DR PRINTS; PR01898; SAGSUPRFAMLY.
DR SUPFAM; SSF50203; SSF50203; 1.
DR SUPFAM; SSF54334; SSF54334; 1.
DR PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Secreted; Signal; Toxin; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..236
FT /note="Exotoxin type H"
FT /id="PRO_0000035603"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:1ET9"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1ET9"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1ET9"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1ET9"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1ET9"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1ET9"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1ET9"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1ET9"
SQ SEQUENCE 236 AA; 27485 MW; 16352923907AD40D CRC64;
MRYNCRYSHI DKKIYSMIIC LSFLLYSNVV QANSYNTTNR HNLESLYKHD SNLIEADSIK
NSPDIVTSHM LKYSVKDKNL SVFFEKDWIS QEFKDKEVDI YALSAQEVCE CPGKRYEAFG
GITLTNSEKK EIKVPVNVWD KSKQQPPMFI TVNKPKVTAQ EVDIKVRKLL IKKYDIYNNR
EQKYSKGTVT LDLNSGKDIV FDLYYFGNGD FNSMLKIYSN NERIDSTQFH VDVSIS