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Q32GM1

- STXA_SHIDS

UniProt

Q32GM1 - STXA_SHIDS

Protein

Shiga toxin subunit A

Gene

stxA

Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      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 By similarity.By similarity

    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
    Sitei273 – 2742Cleavage; 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

    Enzyme and pathway databases

    BioCyciSDYS300267:GJEW-1385-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shiga toxin subunit A (EC:3.2.2.22)
    Gene namesi
    Name:stxA
    Ordered Locus Names:SDY_1389
    OrganismiShigella dysenteriae serotype 1 (strain Sd197)
    Taxonomic identifieri300267 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000002716: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 315293Shiga toxin subunit APRO_0000312303Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi264 ↔ 283By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi300267.SDY_1389.

    Structurei

    3D structure databases

    ProteinModelPortaliQ32GM1.
    SMRiQ32GM1. Positions 23-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 273251A1Add
    BLAST
    Regioni274 – 31542A2Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000010102.
    KOiK11006.
    OrthoDBiEOG6BGNXJ.

    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.

    Q32GM1-1 [UniParc]FASTAAdd to Basket

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    MKIIIFRVLT FFFVIFSVNV VAKEFTLDFS TAKTYVDSLN VIRSAIGTPL    50
    QTISSGGTSL LMIDSGTGDN LFAVDVRGID PEEGRFNNLR LIVERNNLYV 100
    TGFVNRTNNV FYRFADFSHV TFPGTTAVTL SGDSSYTTLQ RVAGISRTGM 150
    QINRHSLTTS YLDLMSHSGT SLTQSVARAM LRFVTVTAEA LRFRQIQRGF 200
    RTTLDDLSGR SYVMTAEDVD LTLNWGRLSS VLPDYHGQDS VRVGRISFGS 250
    INAILGSVAL ILNCHHHASR VARMASDEFP SMCPADGRVR GITHNKILWD 300
    SSTLGAILMR RTISS 315
    Length:315
    Mass (Da):34,814
    Last modified:December 6, 2005 - v1
    Checksum:i8A423DF7ABF58F30
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000034 Genomic DNA. Translation: ABB61534.1.
    RefSeqiYP_403025.1. NC_007606.1.

    Genome annotation databases

    EnsemblBacteriaiABB61534; ABB61534; SDY_1389.
    GeneIDi3796555.
    KEGGisdy:SDY_1389.
    PATRICi18692394. VBIShiDys99784_1650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000034 Genomic DNA. Translation: ABB61534.1 .
    RefSeqi YP_403025.1. NC_007606.1.

    3D structure databases

    ProteinModelPortali Q32GM1.
    SMRi Q32GM1. Positions 23-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300267.SDY_1389.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB61534 ; ABB61534 ; SDY_1389 .
    GeneIDi 3796555.
    KEGGi sdy:SDY_1389.
    PATRICi 18692394. VBIShiDys99784_1650.

    Phylogenomic databases

    HOGENOMi HOG000010102.
    KOi K11006.
    OrthoDBi EOG6BGNXJ.

    Enzyme and pathway databases

    BioCyci SDYS300267:GJEW-1385-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sd197.

    Entry informationi

    Entry nameiSTXA_SHIDS
    AccessioniPrimary (citable) accession number: Q32GM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3