Skip Header

Contribute Send feedback
Read comments (?) or add your own

P08026 (STXA_BPH19) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 64. 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
Synonyms:sltA
OrganismEnterobacteria phage H19B (Bacteriophage H19B)
Taxonomic identifier69932 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambda-like virusesunclassified Lambda-like viruses
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 subnit 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: 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_0000030791

Regions

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

Sites

Active site1891 Ref.3
Site273 – 2742Cleavage; by furin By similarity

Amino acid modifications

Disulfide bond264 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
P08026 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 8B993DF7A8E58F30

FASTA31534,800
        10         20         30         40         50         60 
MKIIIFRVLT FFFVIFSVNV VAKEFTLDFS TAKTYVDSLN VIRSAIGTPL QTISSGGTSL 

        70         80         90        100        110        120 
LMIDSGSGDN 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]"Nucleotide sequence of the Shiga-like toxin genes of Escherichia coli."
Calderwood S.B., Auclair F., Donohue-Rolfe A., Keusch G.T., Mekalanos J.J.
Proc. Natl. Acad. Sci. U.S.A. 84:4364-4368(1987) [PubMed: 3299365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence and promoter mapping of the Escherichia coli Shiga-like toxin operon of bacteriophage H-19B."
de Grandis S., Ginsberg J., Toone M., Climie S., Friesen J., Brunton J.L.
J. Bacteriol. 169:4313-4319(1987) [PubMed: 3040689] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I."
Hovde C.J., Calderwood S.B., Mekalanos J.J., Collier R.J.
Proc. Natl. Acad. Sci. U.S.A. 85:2568-2572(1988) [PubMed: 3357883] [Abstract]
Cited for: ACTIVE SITE.
[4]"Evidence that the A2 fragment of Shiga-like toxin type I is required for holotoxin integrity."
Austin P.R., Jablonski P.E., Bohach G.A., Dunker A.K., Hovde C.J.
Infect. Immun. 62:1768-1775(1994) [PubMed: 8168939] [Abstract]
Cited for: ROLE OF A2 FRAGMENT IN HOLOTOXIN ASSEMBLY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16625 Genomic DNA. Translation: AAA98099.1.
M17358 Genomic DNA. Translation: AAA32229.1.
PIRXUBPH9. A27052.
A53887.

3D structure databases

ProteinModelPortalP08026.
SMRP08026. Positions 23-312.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
PfamPF00161. RIP. 1 hit.
[Graphical view]
PIRSFPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
SUPFAMSSF56371. Ribosome_inactivat_prot. 1 hit.
PROSITEPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSTXA_BPH19
AccessionPrimary (citable) accession number: P08026
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 31, 2011
This is version 64 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