Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10149 (STXA_BPH30) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 1 subunit A

Short name=SLT-1 A subunit
Short name=SLT-1a
Short name=SLT-Ia
EC=3.2.2.22
Alternative name(s):
Verocytotoxin 1 subunit A
Verotoxin 1 subunit A
rRNA N-glycosidase 1
Gene names
Name:stxA
OrganismBacteriophage H30
Taxonomic identifier12371 [NCBI]
Taxonomic lineageVirusesunclassified phages
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 subunit A and five copies of subunit B.

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
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
Chain23 – 315293Shiga-like toxin 1 subunit A
PRO_0000030790

Regions

Region23 – 273251A1 By similarity
Region274 – 31542A2 By similarity

Sites

Active site1891 By similarity
Site273 – 2742Cleavage; by furin By similarity

Amino acid modifications

Disulfide bond264 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
P10149 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8A423DF7ABF58F30

FASTA31534,814
        10         20         30         40         50         60 
MKIIIFRVLT FFFVIFSVNV VAKEFTLDFS TAKTYVDSLN VIRSAIGTPL QTISSGGTSL 

        70         80         90        100        110        120 
LMIDSGTGDN LFAVDVRGID PEEGRFNNLR LIVERNNLYV TGFVNRTNNV FYRFADFSHV 

       130        140        150        160        170        180 
TFPGTTAVTL SGDSSYTTLQ RVAGISRTGM QINRHSLTTS YLDLMSHSGT SLTQSVARAM 

       190        200        210        220        230        240 
LRFVTVTAEA LRFRQIQRGF RTTLDDLSGR SYVMTAEDVD LTLNWGRLSS VLPDYHGQDS 

       250        260        270        280        290        300 
VRVGRISFGS INAILGSVAL ILNCHHHASR VARMASDEFP SMCPADGRVR GITHNKILWD 

       310 
SSTLGAILMR RTISS 

« Hide

References

[1]"The primary structure of the operons coding for Shigella dysenteriae toxin and temperature phage H30 shiga-like toxin."
Kozlov Y.V., Kabishev A.A., Lukyanov E.V., Bayev A.A.
Gene 67:213-221(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23980 Genomic DNA. Translation: AAA72732.1.

3D structure databases

ProteinModelPortalP10149.
SMRP10149. Positions 23-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6144N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameSTXA_BPH30
AccessionPrimary (citable) accession number: P10149
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 72 of the entry and version 1 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