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P09331 (ETA_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exfoliative toxin A

EC=3.4.21.-
Alternative name(s):
Epidermolytic toxin A
Gene names
Name:eta
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS). Ref.4 Ref.5

Cofactor

Calcium.

Sequence similarities

Belongs to the peptidase S1B family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838
Chain39 – 280242Exfoliative toxin A
PRO_0000026905

Sites

Active site1101Charge relay system
Active site1581Charge relay system
Active site2331Charge relay system

Experimental info

Mutagenesis2331S → G: Loss of toxicity. Ref.6

Secondary structure

................................................ 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09331 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 4FBAF750FFE43586

FASTA28031,077
        10         20         30         40         50         60 
MNNSKIISKV LLSLSLFTVG ASAFVIQDEL MQKNHAKAEV SAEEIKKHEE KWNKYYGVNA 

        70         80         90        100        110        120 
FNLPKELFSK VDEKDRQKYP YNTIGNVFVK GQTSATGVLI GKNTVLTNRH IAKFANGDPS 

       130        140        150        160        170        180 
KVSFRPSINT DDNGNTETPY GEYEVKEILQ EPFGAGVDLA LIRLKPDQNG VSLGDKISPA 

       190        200        210        220        230        240 
KIGTSNDLKD GDKLELIGYP FDHKVNQMHR SEIELTTLSR GLRYYGFTVP GNSGSGIFNS 

       250        260        270        280 
NGELVGIHSS KVSHLDREHQ INYGVGIGNY VKRIINEKNE 

« Hide

References

[1]"Sequence determination and comparison of the exfoliative toxin A and toxin B genes from Staphylococcus aureus."
Lee C.Y., Schmidt J.J., Johnson-Winegar A.D., Spero L., Iandolo J.J.
J. Bacteriol. 169:3904-3909(1987) [PubMed: 3040666] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: UT0002.
[2]"Nucleotide sequence of the epidermolytic toxin A gene of Staphylococcus aureus."
O'Toole P.W., Foster T.J.
J. Bacteriol. 169:3910-3915(1987) [PubMed: 3040667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TC16.
[3]"DNA sequencing of the eta gene coding for staphylococcal exfoliative toxin serotype A."
Sakurai S., Suzuki H., Kondo I.
J. Gen. Microbiol. 134:711-717(1988) [PubMed: 3183619] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ZM.
[4]"The reactive serine residue of epidermolytic toxin A."
Bailey C.J., Smith T.P.
Biochem. J. 269:535-537(1990) [PubMed: 2117445] [Abstract]
Cited for: FUNCTION.
[5]"The epidermolytic toxins are serine proteases."
Dancer S.J., Garrat R., Saldanha J., Jhoti H., Evans R.
FEBS Lett. 268:129-132(1990) [PubMed: 2384148] [Abstract]
Cited for: FUNCTION.
[6]"The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus."
Redpath M.B., Foster T.J., Bailey C.J.
FEMS Microbiol. Lett. 65:151-155(1991) [PubMed: 1884990] [Abstract]
Cited for: MUTAGENESIS OF SER-233.
[7]"The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease."
Vath G.M., Earhart C.A., Rago J.V., Kim M.H., Bohach G.A., Schlievert P.M., Ohlendorf D.H.
Biochemistry 36:1559-1566(1997) [PubMed: 9048539] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: MNEV.
[8]"The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7-A resolution."
Cavarelli J., Prevost G., Bourguet W., Moulinier L., Chevrier B., Delagoutte B., Bilwes A., Mourey L., Rifai S., Piemont Y., Moras D.
Structure 5:813-824(1997) [PubMed: 9261066] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17357 Genomic DNA. Translation: AAA26626.1.
M17347 Genomic DNA. Translation: AAA26625.1.
L25372 Genomic DNA. Translation: AAA17490.1.
PIRPRSAEA. A26680.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGJX-ray1.70A/B39-280[»]
1DUAX-ray2.00A39-280[»]
1DUEX-ray2.00A39-280[»]
1EXFX-ray2.10A39-280[»]
ProteinModelPortalP09331.
SMRP09331. Positions 39-280.
ModBaseSearch...

Protein family/group databases

MEROPSS01.270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR000126. Pept_S1B_AS.
IPR001254. Peptidase_S1_S6.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameETA_STAAU
AccessionPrimary (citable) accession number: P09331
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families