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 02-SEP-2026, entry version 128. 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; Bacillati; Bacillota; Bacilli; Caryophanales; 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 FUNCTION, AND MUTAGENESIS OF SER-217. RX PubMed=12093888; DOI=10.1172/jci15766; RA Hanakawa Y., Schechter N.M., Lin C., Garza L., Li H., Yamaguchi T., RA Fudaba Y., Nishifuji K., Sugai M., Amagai M., Stanley J.R.; RT "Molecular mechanisms of blister formation in bullous impetigo and RT staphylococcal scalded skin syndrome."; RL J. Clin. Invest. 110:53-60(2002). RN [6] RP FUNCTION. RX PubMed=12880431; DOI=10.1046/j.1523-1747.2003.12362.x; RA Hanakawa Y., Selwood T., Woo D., Lin C., Schechter N.M., Stanley J.R.; RT "Calcium-dependent conformation of desmoglein 1 is required for its RT cleavage by exfoliative toxin."; RL J. Invest. Dermatol. 121:383-389(2003). RN [7] 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 Protease activity against the host desmosome component protein DSG1, CC resulting in disruption of desmosome-mediated cell-cell adhesion and CC impaired epidermal cell barriers (PubMed:12093888, PubMed:12880431). CC Exfoliative toxins cause impetigous diseases commonly referred as CC staphylococcal scalded skin syndrome (SSSS). CC {ECO:0000269|PubMed:12093888, ECO:0000269|PubMed:12880431, 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; WP_010994026.1; NC_003265.1. DR PDB; 1DT2; X-ray; 2.80 A; A=33-277. DR PDB; 1QTF; X-ray; 2.40 A; A=32-277. DR AlphaFoldDB; P09332; -. DR MDposit; 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:0008236; F:serine-type peptidase activity; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR008256; Peptidase_S1B. DR InterPro; IPR008353; Peptidase_S1B_tx. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR028301; V8_his_AS. DR InterPro; IPR000126; V8_ser_AS. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR01774; EXFOLTOXIN. DR PRINTS; PR00839; V8PROTEASE. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00672; V8_HIS; 1. DR PROSITE; PS00673; V8_SER; 1. DR PDBsum; 1DT2; -. DR PDBsum; 1QTF; -. 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 MUTAGEN 217 FT /note="S->A: Abolishes cleavage of host DSG1." FT /evidence="ECO:0000269|PubMed:12093888" 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 HELIX 165..168 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 //