ETB_STAAU
ID ETB_STAAU Reviewed; 277 AA.
AC P09332;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Exfoliative toxin B;
DE EC=3.4.21.-;
DE AltName: Full=Epidermolytic toxin B;
DE Flags: Precursor;
GN Name=etb;
OS Staphylococcus aureus.
OG Plasmid pRW001.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3733674; DOI=10.1128/jb.167.2.726-728.1986;
RA Jackson M.P., Iandolo J.J.;
RT "Sequence of the exfoliative toxin B gene of Staphylococcus aureus.";
RL J. Bacteriol. 167:726-728(1986).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION.
RC STRAIN=UT0002;
RX PubMed=3040666; DOI=10.1128/jb.169.9.3904-3909.1987;
RA Lee C.Y., Schmidt J.J., Johnson-Winegar A.D., Spero L., Iandolo J.J.;
RT "Sequence determination and comparison of the exfoliative toxin A and toxin
RT B genes from Staphylococcus aureus.";
RL J. Bacteriol. 169:3904-3909(1987).
RN [3]
RP FUNCTION.
RX PubMed=2117445; DOI=10.1042/bj2690535;
RA Bailey C.J., Smith T.P.;
RT "The reactive serine residue of epidermolytic toxin A.";
RL Biochem. J. 269:535-537(1990).
RN [4]
RP FUNCTION.
RX PubMed=2384148; DOI=10.1016/0014-5793(90)80990-z;
RA Dancer S.J., Garrat R., Saldanha J., Jhoti H., Evans R.;
RT "The epidermolytic toxins are serine proteases.";
RL FEBS Lett. 268:129-132(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 33-277.
RX PubMed=10752623; DOI=10.1110/ps.9.3.610;
RA Papageorgiou A.C., Plano L.R., Collins C.M., Acharya K.R.;
RT "Structural similarities and differences in Staphylococcus aureus
RT exfoliative toxins A and B as revealed by their crystal structures.";
RL Protein Sci. 9:610-618(2000).
CC -!- FUNCTION: Has serine protease-like properties and binds to the skin
CC protein profilaggrin. Cleaves substrates after acidic residues.
CC Exfoliative toxins cause impetigous diseases commonly referred as
CC staphylococcal scalded skin syndrome (SSSS).
CC {ECO:0000269|PubMed:2117445, ECO:0000269|PubMed:2384148}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17348; AAA26628.1; -; Genomic_DNA.
DR PIR; A26050; A26050.
DR PIR; B26680; PRSAEB.
DR RefSeq; NP_478350.1; NC_003265.1.
DR RefSeq; WP_010994026.1; NZ_WKGU01000048.1.
DR RefSeq; YP_006938189.1; NC_013334.1.
DR RefSeq; YP_008709833.1; NC_022598.1.
DR PDB; 1DT2; X-ray; 2.80 A; A=33-277.
DR PDB; 1QTF; X-ray; 2.40 A; A=32-277.
DR PDBsum; 1DT2; -.
DR PDBsum; 1QTF; -.
DR AlphaFoldDB; P09332; -.
DR SMR; P09332; -.
DR MEROPS; S01.270; -.
DR EvolutionaryTrace; P09332; -.
DR PRO; PR:P09332; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR008353; Peptidase_S1B_tx.
DR InterPro; IPR028301; V8_his_AS.
DR InterPro; IPR000126; V8_ser_AS.
DR PRINTS; PR01774; EXFOLTOXIN.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00672; V8_HIS; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Plasmid; Protease;
KW Serine protease; Signal; Toxin; Virulence.
FT SIGNAL 1..31
FT CHAIN 32..277
FT /note="Exfoliative toxin B"
FT /id="PRO_0000026906"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 196..210
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1QTF"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1QTF"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1QTF"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:1QTF"
SQ SEQUENCE 277 AA; 30765 MW; DE1A7BEE273CF92F CRC64;
MDKNMFKKII LAASIFTISL PVIPFESTLQ AKEYSAEEIR KLKQKFEVPP TDKELYTHIT
DNARSPYNSV GTVFVKGSTL ATGVLIGKNT IVTNYHVARE AAKNPSNIIF TPAQNRDAEK
NEFPTPYGKF EAEEIKESPY GQGLDLAIIK LKPNEKGESA GDLIQPANIP DHIDIQKGDK
YSLLGYPYNY SAYSLYQSQI EMFNDSQYFG YTEVGNSGSG IFNLKGELIG IHSGKGGQHN
LPIGVFFNRK ISSLYSVDNT FGDTLGNDLK KRAKLDK
