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Protein

Exfoliative toxin A

Gene

eta

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei110Charge relay system1
Active sitei158Charge relay system1
Active sitei233Charge relay system1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease, Toxin

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiS01.270.

Names & Taxonomyi

Protein namesi
Recommended name:
Exfoliative toxin A (EC:3.4.21.-)
Alternative name(s):
Epidermolytic toxin A
Gene namesi
Name:eta
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi233S → G: Loss of toxicity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Add BLAST38
ChainiPRO_000002690539 – 280Exfoliative toxin AAdd BLAST242

Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 56Combined sources15
Helixi60 – 62Combined sources3
Turni65 – 67Combined sources3
Beta strandi68 – 70Combined sources3
Helixi75 – 77Combined sources3
Helixi81 – 83Combined sources3
Beta strandi84 – 89Combined sources6
Turni90 – 92Combined sources3
Beta strandi93 – 99Combined sources7
Beta strandi101 – 107Combined sources7
Helixi109 – 112Combined sources4
Helixi113 – 115Combined sources3
Helixi119 – 121Combined sources3
Beta strandi122 – 126Combined sources5
Beta strandi143 – 150Combined sources8
Beta strandi160 – 164Combined sources5
Helixi173 – 176Combined sources4
Helixi185 – 187Combined sources3
Beta strandi193 – 198Combined sources6
Turni201 – 203Combined sources3
Beta strandi209 – 215Combined sources7
Helixi218 – 220Combined sources3
Beta strandi221 – 225Combined sources5
Helixi230 – 232Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi242 – 253Combined sources12
Beta strandi260 – 266Combined sources7
Helixi269 – 278Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGJX-ray1.70A/B39-280[»]
1DUAX-ray2.00A39-280[»]
1DUEX-ray2.00A39-280[»]
1EXFX-ray2.10A39-280[»]
ProteinModelPortaliP09331.
SMRiP09331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09331.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S1B family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR028301. V8_his_AS.
IPR000126. V8_ser_AS.
[Graphical view]
PRINTSiPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNSKIISKV LLSLSLFTVG ASAFVIQDEL MQKNHAKAEV SAEEIKKHEE
60 70 80 90 100
KWNKYYGVNA FNLPKELFSK VDEKDRQKYP YNTIGNVFVK GQTSATGVLI
110 120 130 140 150
GKNTVLTNRH IAKFANGDPS KVSFRPSINT DDNGNTETPY GEYEVKEILQ
160 170 180 190 200
EPFGAGVDLA LIRLKPDQNG VSLGDKISPA KIGTSNDLKD GDKLELIGYP
210 220 230 240 250
FDHKVNQMHR SEIELTTLSR GLRYYGFTVP GNSGSGIFNS NGELVGIHSS
260 270 280
KVSHLDREHQ INYGVGIGNY VKRIINEKNE
Length:280
Mass (Da):31,077
Last modified:July 1, 1989 - v1
Checksum:i4FBAF750FFE43586
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17357 Genomic DNA. Translation: AAA26626.1.
M17347 Genomic DNA. Translation: AAA26625.1.
L25372 Genomic DNA. Translation: AAA17490.1.
PIRiA26680. PRSAEA.
RefSeqiWP_001065781.1. NZ_MCFM01000004.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17357 Genomic DNA. Translation: AAA26626.1.
M17347 Genomic DNA. Translation: AAA26625.1.
L25372 Genomic DNA. Translation: AAA17490.1.
PIRiA26680. PRSAEA.
RefSeqiWP_001065781.1. NZ_MCFM01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGJX-ray1.70A/B39-280[»]
1DUAX-ray2.00A39-280[»]
1DUEX-ray2.00A39-280[»]
1EXFX-ray2.10A39-280[»]
ProteinModelPortaliP09331.
SMRiP09331.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP09331.
PROiP09331.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR028301. V8_his_AS.
IPR000126. V8_ser_AS.
[Graphical view]
PRINTSiPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00672. V8_HIS. 1 hit.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiETA_STAAU
AccessioniPrimary (citable) accession number: P09331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.