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P09332 (ETB_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 B

EC=3.4.21.-
Alternative name(s):
Epidermolytic toxin B
Gene names
Name:etb
Encoded onPlasmid pRW001
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length277 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.3 Ref.4

Sequence similarities

Belongs to the peptidase S1B family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   Technical term3D-structure
Direct protein sequencing
Plasmid
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 – 3131
Chain32 – 277246Exfoliative toxin B
PRO_0000026906

Sites

Active site961Charge relay system By similarity
Active site1451Charge relay system By similarity
Active site2171Charge relay system By similarity

Secondary structure

............................................. 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09332 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: DE1A7BEE273CF92F

FASTA27730,765
        10         20         30         40         50         60 
MDKNMFKKII LAASIFTISL PVIPFESTLQ AKEYSAEEIR KLKQKFEVPP TDKELYTHIT 

        70         80         90        100        110        120 
DNARSPYNSV GTVFVKGSTL ATGVLIGKNT IVTNYHVARE AAKNPSNIIF TPAQNRDAEK 

       130        140        150        160        170        180 
NEFPTPYGKF EAEEIKESPY GQGLDLAIIK LKPNEKGESA GDLIQPANIP DHIDIQKGDK 

       190        200        210        220        230        240 
YSLLGYPYNY SAYSLYQSQI EMFNDSQYFG YTEVGNSGSG IFNLKGELIG IHSGKGGQHN 

       250        260        270 
LPIGVFFNRK ISSLYSVDNT FGDTLGNDLK KRAKLDK 

« Hide

References

[1]"Sequence of the exfoliative toxin B gene of Staphylococcus aureus."
Jackson M.P., Iandolo J.J.
J. Bacteriol. 167:726-728(1986) [PubMed: 3733674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION.
Strain: UT0002.
[3]"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.
[4]"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.
[5]"Structural similarities and differences in Staphylococcus aureus exfoliative toxins A and B as revealed by their crystal structures."
Papageorgiou A.C., Plano L.R., Collins C.M., Acharya K.R.
Protein Sci. 9:610-618(2000) [PubMed: 10752623] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 33-277.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17348 Genomic DNA. Translation: AAA26628.1.
PIRA26050.
PRSAEB. B26680.
RefSeqNP_478350.1. NC_003265.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DT2X-ray2.80A33-277[»]
1QTFX-ray2.40A32-277[»]
ProteinModelPortalP09332.
SMRP09332. Positions 33-277.
ModBaseSearch...

Protein family/group databases

MEROPSS01.270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4594894.

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.
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameETB_STAAU
AccessionPrimary (citable) accession number: P09332
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