ETA_STAAU
ID ETA_STAAU Reviewed; 280 AA.
AC P09331;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Exfoliative toxin A;
DE EC=3.4.21.-;
DE AltName: Full=Epidermolytic toxin A;
DE Flags: Precursor;
GN Name=eta;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TC16;
RX PubMed=3040667; DOI=10.1128/jb.169.9.3910-3915.1987;
RA O'Toole P.W., Foster T.J.;
RT "Nucleotide sequence of the epidermolytic toxin A gene of Staphylococcus
RT aureus.";
RL J. Bacteriol. 169:3910-3915(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZM;
RX PubMed=3183619; DOI=10.1099/00221287-134-3-711;
RA Sakurai S., Suzuki H., Kondo I.;
RT "DNA sequencing of the eta gene coding for staphylococcal exfoliative toxin
RT serotype A.";
RL J. Gen. Microbiol. 134:711-717(1988).
RN [4]
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 [5]
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 [6]
RP MUTAGENESIS OF SER-233.
RX PubMed=1884990; DOI=10.1016/0378-1097(91)90295-l;
RA Redpath M.B., Foster T.J., Bailey C.J.;
RT "The role of the serine protease active site in the mode of action of
RT epidermolytic toxin of Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 65:151-155(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=MNEV;
RX PubMed=9048539; DOI=10.1021/bi962614f;
RA Vath G.M., Earhart C.A., Rago J.V., Kim M.H., Bohach G.A., Schlievert P.M.,
RA Ohlendorf D.H.;
RT "The structure of the superantigen exfoliative toxin A suggests a novel
RT regulation as a serine protease.";
RL Biochemistry 36:1559-1566(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9261066; DOI=10.1016/s0969-2126(97)00235-9;
RA Cavarelli J., Prevost G., Bourguet W., Moulinier L., Chevrier B.,
RA Delagoutte B., Bilwes A., Mourey L., Rifai S., Piemont Y., Moras D.;
RT "The structure of Staphylococcus aureus epidermolytic toxin A, an atypic
RT serine protease, at 1.7-A resolution.";
RL Structure 5:813-824(1997).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR EMBL; M17357; AAA26626.1; -; Genomic_DNA.
DR EMBL; M17347; AAA26625.1; -; Genomic_DNA.
DR EMBL; L25372; AAA17490.1; -; Genomic_DNA.
DR PIR; A26680; PRSAEA.
DR RefSeq; WP_001065781.1; NZ_WKGU01000030.1.
DR PDB; 1AGJ; X-ray; 1.70 A; A/B=39-280.
DR PDB; 1DUA; X-ray; 2.00 A; A=39-280.
DR PDB; 1DUE; X-ray; 2.00 A; A=39-280.
DR PDB; 1EXF; X-ray; 2.10 A; A=39-280.
DR PDBsum; 1AGJ; -.
DR PDBsum; 1DUA; -.
DR PDBsum; 1DUE; -.
DR PDBsum; 1EXF; -.
DR AlphaFoldDB; P09331; -.
DR SMR; P09331; -.
DR MEROPS; S01.270; -.
DR EvolutionaryTrace; P09331; -.
DR PRO; PR:P09331; -.
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; Calcium; Direct protein sequencing; Hydrolase; Protease;
KW Serine protease; Signal; Toxin; Virulence.
FT SIGNAL 1..38
FT CHAIN 39..280
FT /note="Exfoliative toxin A"
FT /id="PRO_0000026905"
FT ACT_SITE 110
FT /note="Charge relay system"
FT ACT_SITE 158
FT /note="Charge relay system"
FT ACT_SITE 233
FT /note="Charge relay system"
FT MUTAGEN 233
FT /note="S->G: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:1884990"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1AGJ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1AGJ"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1EXF"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:1AGJ"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:1AGJ"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:1AGJ"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1AGJ"
SQ SEQUENCE 280 AA; 31077 MW; 4FBAF750FFE43586 CRC64;
MNNSKIISKV LLSLSLFTVG ASAFVIQDEL MQKNHAKAEV SAEEIKKHEE KWNKYYGVNA
FNLPKELFSK VDEKDRQKYP YNTIGNVFVK GQTSATGVLI GKNTVLTNRH IAKFANGDPS
KVSFRPSINT DDNGNTETPY GEYEVKEILQ EPFGAGVDLA LIRLKPDQNG VSLGDKISPA
KIGTSNDLKD GDKLELIGYP FDHKVNQMHR SEIELTTLSR GLRYYGFTVP GNSGSGIFNS
NGELVGIHSS KVSHLDREHQ INYGVGIGNY VKRIINEKNE
