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P09385 (STXA_BP933) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Shiga-like toxin 2 subunit A

Short name=SLT-2 A subunit
Short name=SLT-2a
Short name=SLT-IIa
EC=3.2.2.22
Alternative name(s):
Verocytotoxin 2 subunit A
Verotoxin 2 subunit A
rRNA N-glycosidase 2
Gene names
Name:stxA2
Synonyms:stx2A
Ordered Locus Names:L0103
OrganismEnterobacteria phage 933W (Bacteriophage 933W) [Complete proteome]
Taxonomic identifier10730 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridae
Virus hostEscherichia coli O157:H7 [TaxID: 83334]

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Subunit structure

Shiga-like toxin contains a single A subunit and multiple copies of a B subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribosome-inactivating protein family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protein synthesis inhibitor
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processnegative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionrRNA N-glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 319297Shiga-like toxin 2 subunit A
PRO_0000030792

Regions

Region23 – 272250A1 By similarity
Region273 – 31442A2 By similarity

Sites

Active site1891 By similarity
Site272 – 2732Cleavage; by furin By similarity

Amino acid modifications

Disulfide bond263 ↔ 282

Natural variations

Natural variant171S → P in strain: OX3:H21.
Natural variant261T → M in strain: OX3:H21.
Natural variant2771E → D in strain: FLY16 and CS1718.

Secondary structure

...................................................... 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09385 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 98F73319ACAE48D6

FASTA31935,714
        10         20         30         40         50         60 
MKCILFKWVL CLLLGFSSVS YSREFTIDFS TQQSYVSSLN SIRTEISTPL EHISQGTTSV 

        70         80         90        100        110        120 
SVINHTPPGS YFAVDIRGLD VYQARFDHLR LIIEQNNLYV AGFVNTATNT FYRFSDFTHI 

       130        140        150        160        170        180 
SVPGVTTVSM TTDSSYTTLQ RVAALERSGM QISRHSLVSS YLALMEFSGN TMTRDASRAV 

       190        200        210        220        230        240 
LRFVTVTAEA LRFRQIQREF RQALSETAPV YTMTPGDVDL TLNWGRISNV LPEYRGEDGV 

       250        260        270        280        290        300 
RVGRISFNNI SAILGTVAVI LNCHHQGARS VRAVNEESQP ECQITGDRPV IKINNTLWES 

       310 
NTAAAFLNRK SQFLYTTGK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli 933."
Jackson M.P., Neill R.J., O'Brien A.D., Holmes R.K., Newland J.W.
FEMS Microbiol. Lett. 44:109-114(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Two copies of Shiga-like toxin II-related genes common in enterohemorrhagic Escherichia coli strains are responsible for the antigenic heterogeneity of the O157:H-strain E32511."
Schmitt C.K., McKee M.L., O'Brien A.D.
Infect. Immun. 59:1065-1073(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: E32511.
[3]"Polymerase chain reaction amplification, cloning and sequencing of variant Escherichia coli Shiga-like toxin type II operons."
Paton A.W., Paton J.C., Manning P.A.
Microb. Pathog. 15:77-82(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: OX3:H21.
[4]"An ileX tRNA gene is located close to the Shiga toxin II operon in enterohemorrhagic Escherichia coli O157 and non-O157 strains."
Schmidt H., Scheef J., Janetzki-Mittmann C., Datz M., Karch H.
FEMS Microbiol. Lett. 149:39-44(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Identification of an insertion sequence, IS1203 variant, in a Shiga toxin 2 gene of Escherichia coli O157:H7."
Kusumoto M., Nishiya Y., Kawamura Y., Shinagawa K.
J. Biosci. Bioeng. 87:93-96(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Detection of Escherichia coli O157:H7 from Musca domestica (Diptera: Muscidae) at a cattle farm in Japan."
Iwasa M., Makino S., Asakura H., Kobori H., Morimoto Y.
J. Med. Entomol. 36:108-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FLY16.
[7]"Characterization of Shiga toxin genes in Shiga toxin-producing Escherichia coli isolated in Korea."
Yu J.Y., Jeon H.G., Kang Y.H., Kim E.C., Sohn C.K., Lee B.K.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CS1718.
[8]"Phylogenetic diversity and similarity of active sites of Shiga toxin (stx) in Shiga toxin-producing Escherichia coli (STEC) isolates from humans and animals."
Asakura H., Makino S., Kobori H., Watarai M., Shirahata T., Ikeda T., Takeshi K.
Epidemiol. Infect. 127:27-36(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Genetic typing of shiga toxin 2 variants of Escherichia coli by PCR-restriction fragment length polymorphism analysis."
De Baets L., Van der Taelen I., De Filette M., Pierard D., Allison L., De Greve H., Hernalsteens J.P., Imberechts H.
Appl. Environ. Microbiol. 70:6309-6314(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga toxin as a phage late-gene product."
Plunkett G. III, Rose D.J., Durfee T.J., Blattner F.R.
J. Bacteriol. 181:1767-1778(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"Regulation of the Shiga-like toxin II operon in Escherichia coli."
Muhldorfer I., Hacker J., Keusch G.T., Acheson D.W., Tschape H., Kane A.V., Ritter A., Olschlager T., Donohue-Rolfe A.
Infect. Immun. 64:495-502(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7."
Fraser M.E., Fujinaga M., Cherney M.M., Melton-Celsa A.R., Twiddy E.M., O'Brien A.D., James M.N.G.
J. Biol. Chem. 279:27511-27517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 23-319.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07865 Genomic DNA. Translation: CAA30714.1.
M59432 Unassigned DNA. Translation: AAA19623.1.
L11079 Unassigned DNA. Translation: AAA16362.1.
Y10775 Genomic DNA. Translation: CAA71747.1.
AB017524 Genomic DNA. Translation: BAA33759.1.
AB015057 Genomic DNA. Translation: BAA34372.1.
AF461167 Genomic DNA. Translation: AAM70033.1.
AB048239 Genomic DNA. Translation: BAB83026.1.
AB048240 Genomic DNA. Translation: BAB83028.1.
AY443052 Genomic DNA. Translation: AAS07596.1.
AF125520 Genomic DNA. Translation: AAD25445.1.
PIRI76713.
S01032.
RefSeqNP_049500.1. NC_000924.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4PX-ray1.77A23-319[»]
2GA4X-ray1.80A23-319[»]
ProteinModelPortalP09385.
SMRP09385. Positions 23-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP09385. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1261950.

Phylogenomic databases

ProtClustDBCLSP2343974.

Family and domain databases

Gene3D3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR016331. Shiga-like_toxin_subunit_A.
[Graphical view]
PfamPF00161. RIP. 1 hit.
[Graphical view]
PIRSFPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
SUPFAMSSF56371. SSF56371. 1 hit.
PROSITEPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09385.

Entry information

Entry nameSTXA_BP933
AccessionPrimary (citable) accession number: P09385
Secondary accession number(s): Q9R398
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references