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Q32GM1 (STXA_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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 toxin subunit A

EC=3.2.2.22
Gene names
Name:stxA
Ordered Locus Names:SDY_1389
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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 By similarity.

Catalytic activity

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

Subunit structure

Shiga toxin contains a single subunit A and five copies of subunit B By similarity.

Sequence similarities

Belongs to the ribosome-inactivating protein family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protein synthesis inhibitor
Toxin
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 315293Shiga toxin subunit A
PRO_0000312303

Regions

Region23 – 273251A1
Region274 – 31542A2

Sites

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

Amino acid modifications

Disulfide bond264 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q32GM1 [UniParc].

Last modified December 6, 2005. 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]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000034 Genomic DNA. Translation: ABB61534.1.
RefSeqYP_403025.1. NC_007606.1.

3D structure databases

ProteinModelPortalQ32GM1.
SMRQ32GM1. Positions 23-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300267.SDY_1389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB61534; ABB61534; SDY_1389.
GeneID3796555.
KEGGsdy:SDY_1389.
PATRIC18692394. VBIShiDys99784_1650.

Phylogenomic databases

HOGENOMHOG000010102.
KOK11006.
OrthoDBEOG6BGNXJ.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-1385-MONOMER.

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_SHIDS
AccessionPrimary (citable) accession number: Q32GM1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families