P09385 (STXA_BP933) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Enterobacteria phage 933W (Bacteriophage 933W) [Complete proteome]

Taxonomic identifier

10730 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › unclassified Podoviridae › Enterobacteria phage 933W sensu lato

Virus host

Escherichia coli O157:H7 [TaxID: 83334]

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	rRNA N-glycosylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 319

297

Shiga-like toxin 2 subunit A

PRO_0000030792

Regions

Region

23 – 272

250

A1 By similarity

Region

273 – 314

42

A2 By similarity

Sites

Active site

189

1

By similarity

Site

272 – 273

2

Cleavage; by furin By similarity

Amino acid modifications

Disulfide bond

263 ↔ 282

Natural variations

Natural variant

17

1

S → P in strain: OX3:H21.

Natural variant

26

1

T → M in strain: OX3:H21.

Natural variant

277

1

E → D in strain: FLY16 and CS1718.

Secondary structure

1

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319

Helix Strand Turn

Details...

Beta strand

24 – 28

5

Helix

32 – 46

15

Beta strand

47 – 55

9

Beta strand

58 – 63

6

Beta strand

71 – 77

7

Beta strand

89 – 94

6

Turn

95 – 97

3

Beta strand

100 – 105

6

Turn

106 – 109

4

Beta strand

110 – 113

4

Helix

115 – 117

3

Beta strand

125 – 129

5

Helix

136 – 143

8

Helix

154 – 166

13

Beta strand

169 – 171

3

Helix

174 – 186

13

Helix

188 – 192

5

Helix

194 – 201

8

Helix

202 – 204

3

Helix

215 – 222

8

Helix

224 – 230

7

Helix

231 – 233

3

Beta strand

240 – 242

3

Beta strand

245 – 247

3

Helix

250 – 256

7

Beta strand

284 – 287

4

Beta strand

290 – 293

4

Beta strand

296 – 299

4

Helix

300 – 306

7

Helix

312 – 317

6

Sequences

	Sequence		Length	Mass (Da)
	P09385 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 98F73319ACAE48D6	FASTA	319	35,714
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

I76713.
S01032.

RefSeq

NP_049500.1. NC_000924.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R4P	X-ray	1.77	A	23-319	[»]
2GA4	X-ray	1.80	A	23-319	[»]

ProteinModelPortal

P09385.

SMR

P09385. Positions 23-319.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09385. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1261950.

Phylogenomic databases

ProtClustDB

CLSP2343974.

Family and domain databases

Gene3D

3.40.420.10. 1 hit.
4.10.470.10. 1 hit.

InterPro

IPR001574. 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]

Pfam

PF00161. RIP. 1 hit.
[Graphical view]

PIRSF

PIRSF001924. Shigella_toxin_subunit_A. 1 hit.

SUPFAM

SSF56371. Ribosome_inactivat_prot. 1 hit.

PROSITE

PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09385.

Entry information

Entry name

STXA_BP933

Accession

Primary (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:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program