P09332 (ETB_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exfoliative toxin B
EC=3.4.21.-

Alternative name(s):
Epidermolytic toxin B

Gene names

Name:

etb

Encoded on

Plasmid pRW001

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Signal
Molecular function	Hydrolase Protease Serine protease Toxin
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Chain

32 – 277

246

Exfoliative toxin B

PRO_0000026906

Sites

Active site

96

1

Charge relay system By similarity

Active site

145

1

Charge relay system By similarity

Active site

217

1

Charge relay system By similarity

Secondary structure

1

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277

Helix Strand Turn

Details...

Helix

36 – 45

10

Turn

53 – 55

3

Beta strand

56 – 58

3

Helix

67 – 69

3

Beta strand

70 – 75

6

Turn

76 – 78

3

Beta strand

79 – 87

9

Beta strand

90 – 93

4

Helix

95 – 98

4

Helix

99 – 101

3

Helix

105 – 107

3

Beta strand

108 – 112

5

Turn

118 – 121

4

Beta strand

130 – 137

8

Beta strand

147 – 151

5

Helix

160 – 163

4

Beta strand

180 – 185

6

Turn

188 – 190

3

Beta strand

196 – 210

15

Helix

214 – 216

3

Beta strand

220 – 222

3

Beta strand

228 – 236

9

Turn

237 – 240

4

Beta strand

241 – 246

6

Turn

253 – 255

3

Helix

265 – 274

10

Sequences

	Sequence		Length	Mass (Da)
	P09332 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: DE1A7BEE273CF92F	FASTA	277	30,765
	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

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.

PIR

A26050.
PRSAEB. B26680.

RefSeq

NP_478350.1. NC_003265.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DT2	X-ray	2.80	A	33-277	[»]
1QTF	X-ray	2.40	A	32-277	[»]

ProteinModelPortal

P09332.

SMR

P09332. Positions 33-277.

ModBase

Search...

Protein family/group databases

MEROPS

S01.270.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

4594894.

Family and domain databases

InterPro

IPR009003. Pept_cys/ser_Trypsin-like.
IPR000126. Pept_S1B_AS.
IPR001254. Peptidase_S1_S6.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ETB_STAAU

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program