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P09385

- STXA_BP933

UniProt

P09385 - STXA_BP933

Protein

Shiga-like toxin 2 subunit A

Gene

stxA2

Organism
Enterobacteria phage 933W (Bacteriophage 933W)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei189 – 1891By similarity
    Sitei272 – 2732Cleavage; by furinBy similarity

    GO - Molecular functioni

    1. rRNA N-glycosylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. negative regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein synthesis inhibitor, Toxin

    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]
    ProteomesiUP000002135: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 319297Shiga-like toxin 2 subunit APRO_0000030792Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi263 ↔ 282

    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 interaction.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 285
    Helixi32 – 4615
    Beta strandi47 – 559
    Beta strandi58 – 636
    Beta strandi71 – 777
    Beta strandi89 – 946
    Turni95 – 973
    Beta strandi100 – 1056
    Turni106 – 1094
    Beta strandi110 – 1134
    Helixi115 – 1173
    Beta strandi125 – 1295
    Helixi136 – 1438
    Helixi154 – 16613
    Beta strandi169 – 1713
    Helixi174 – 18613
    Helixi188 – 1925
    Helixi194 – 2018
    Helixi202 – 2043
    Helixi215 – 2228
    Helixi224 – 2307
    Helixi231 – 2333
    Beta strandi240 – 2423
    Beta strandi245 – 2473
    Helixi250 – 2567
    Beta strandi284 – 2874
    Beta strandi290 – 2934
    Beta strandi296 – 2994
    Helixi300 – 3067
    Helixi312 – 3176

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R4PX-ray1.77A23-319[»]
    2GA4X-ray1.80A23-319[»]
    ProteinModelPortaliP09385.
    SMRiP09385. Positions 23-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09385.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 272250A1By similarityAdd
    BLAST
    Regioni273 – 31442A2By similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    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

    MKCILFKWVL CLLLGFSSVS YSREFTIDFS TQQSYVSSLN SIRTEISTPL    50
    EHISQGTTSV SVINHTPPGS YFAVDIRGLD VYQARFDHLR LIIEQNNLYV 100
    AGFVNTATNT FYRFSDFTHI SVPGVTTVSM TTDSSYTTLQ RVAALERSGM 150
    QISRHSLVSS YLALMEFSGN TMTRDASRAV LRFVTVTAEA LRFRQIQREF 200
    RQALSETAPV YTMTPGDVDL TLNWGRISNV LPEYRGEDGV RVGRISFNNI 250
    SAILGTVAVI LNCHHQGARS VRAVNEESQP ECQITGDRPV IKINNTLWES 300
    NTAAAFLNRK SQFLYTTGK 319
    Length:319
    Mass (Da):35,714
    Last modified:February 1, 1996 - v2
    Checksum:i98F73319ACAE48D6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171S → P in strain: OX3:H21.
    Natural varianti26 – 261T → M in strain: OX3:H21.
    Natural varianti277 – 2771E → D in strain: FLY16 and CS1718.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi I76713.
    S01032.
    RefSeqi NP_049500.1. NC_000924.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R4P X-ray 1.77 A 23-319 [» ]
    2GA4 X-ray 1.80 A 23-319 [» ]
    ProteinModelPortali P09385.
    SMRi P09385. Positions 23-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P09385. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1261950.

    Miscellaneous databases

    EvolutionaryTracei P09385.

    Family and domain databases

    Gene3Di 3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProi 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 ]
    Pfami PF00161. RIP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001924. Shigella_toxin_subunit_A. 1 hit.
    SUPFAMi SSF56371. SSF56371. 1 hit.
    PROSITEi PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 23-319.

    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: October 1, 2014
    This is version 89 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3