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Protein

Shiga-like toxin 2 subunit A

Gene

stxA2

Organism
Enterobacteria phage 933W (Bacteriophage 933W)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei189By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin, Viral exotoxin

Keywords - Biological processi

Modulation of host virulence by virus, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Shiga-like toxin 2 subunit A (EC:3.2.2.22)
Short name:
SLT-2 A subunit
Short name:
SLT-2a
Short name:
SLT-IIa
Alternative name(s):
Verocytotoxin 2 subunit A
Verotoxin 2 subunit A
rRNA N-glycosidase 2
Gene namesi
Name:stxA2
Synonyms:stx2A
Ordered Locus Names:L0103
OrganismiEnterobacteria phage 933W (Bacteriophage 933W)
Taxonomic identifieri10730 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridae
Virus hostiEscherichia coli O157:H7 [TaxID: 83334]
Proteomesi
  • UP000002135 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000003079223 – 319Shiga-like toxin 2 subunit AAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi263 ↔ 282

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei272 – 273Cleavage; by furinBy similarity2

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP09385. 1 interactor.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 28Combined sources5
Helixi32 – 46Combined sources15
Beta strandi47 – 55Combined sources9
Beta strandi58 – 63Combined sources6
Beta strandi71 – 77Combined sources7
Beta strandi89 – 94Combined sources6
Turni95 – 97Combined sources3
Beta strandi100 – 105Combined sources6
Turni106 – 109Combined sources4
Beta strandi110 – 113Combined sources4
Helixi115 – 117Combined sources3
Beta strandi125 – 129Combined sources5
Helixi136 – 143Combined sources8
Helixi154 – 166Combined sources13
Beta strandi169 – 171Combined sources3
Helixi174 – 186Combined sources13
Helixi188 – 192Combined sources5
Helixi194 – 201Combined sources8
Helixi202 – 204Combined sources3
Helixi215 – 222Combined sources8
Helixi224 – 230Combined sources7
Helixi231 – 233Combined sources3
Beta strandi240 – 242Combined sources3
Beta strandi245 – 247Combined sources3
Helixi250 – 256Combined sources7
Beta strandi284 – 287Combined sources4
Beta strandi290 – 293Combined sources4
Beta strandi296 – 299Combined sources4
Helixi300 – 306Combined sources7
Helixi312 – 317Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4PX-ray1.77A23-319[»]
2GA4X-ray1.80A23-319[»]
ProteinModelPortaliP09385.
SMRiP09385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09385.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 272A1By similarityAdd BLAST250
Regioni273 – 314A2By similarityAdd BLAST42

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK11006.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. 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]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PIRSFiPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCILFKWVL CLLLGFSSVS YSREFTIDFS TQQSYVSSLN SIRTEISTPL
60 70 80 90 100
EHISQGTTSV SVINHTPPGS YFAVDIRGLD VYQARFDHLR LIIEQNNLYV
110 120 130 140 150
AGFVNTATNT FYRFSDFTHI SVPGVTTVSM TTDSSYTTLQ RVAALERSGM
160 170 180 190 200
QISRHSLVSS YLALMEFSGN TMTRDASRAV LRFVTVTAEA LRFRQIQREF
210 220 230 240 250
RQALSETAPV YTMTPGDVDL TLNWGRISNV LPEYRGEDGV RVGRISFNNI
260 270 280 290 300
SAILGTVAVI LNCHHQGARS VRAVNEESQP ECQITGDRPV IKINNTLWES
310
NTAAAFLNRK SQFLYTTGK
Length:319
Mass (Da):35,714
Last modified:February 1, 1996 - v2
Checksum:i98F73319ACAE48D6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti17S → P in strain: OX3:H21. 1
Natural varianti26T → M in strain: OX3:H21. 1
Natural varianti277E → D in strain: FLY16 and CS1718. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI76713.
S01032.
RefSeqiNP_049500.1. NC_000924.1.

Genome annotation databases

GeneIDi1261950.
KEGGivg:1261950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI76713.
S01032.
RefSeqiNP_049500.1. NC_000924.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4PX-ray1.77A23-319[»]
2GA4X-ray1.80A23-319[»]
ProteinModelPortaliP09385.
SMRiP09385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09385. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1261950.
KEGGivg:1261950.

Phylogenomic databases

KOiK11006.

Miscellaneous databases

EvolutionaryTraceiP09385.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. 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]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PIRSFiPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTXA_BP933
AccessioniPrimary (citable) accession number: P09385
Secondary accession number(s): Q9R398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.