P0DUJ7 · SSEK3_SALTS

Function

function

Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling and apoptosis (PubMed:26394407, PubMed:28069818, PubMed:28522607, PubMed:29449376, PubMed:32766249).
Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as TRADD, TNFRSF1A/TNFR1 and TNFRSF10B/TRAILR2: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:28069818, PubMed:29449376, PubMed:30902834, PubMed:32766249).
Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab GTPase (Rab1, Rab5 and Rab11), thereby preventing GTPase activity and leading to impaired host vesicular protein transport (PubMed:32504010, PubMed:32974215).
Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32432056).

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site51-53UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site75UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site224-227UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site228Mn2+ (UniProtKB | ChEBI)
Active site258Proton acceptor
Binding site325Mn2+ (UniProtKB | ChEBI)
Binding site327Mn2+ (UniProtKB | ChEBI)
Binding site327UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site332-335UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell
Cellular Componenthost cell Golgi apparatus
Molecular Functionlipid binding
Molecular Functionmanganese ion binding
Molecular Functionprotein-arginine N-acetylglucosaminyltransferase activity
Molecular Functiontoxin activity
Biological Processsymbiont-mediated perturbation of host defense-related programmed cell death

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein-arginine N-acetylglucosaminyltransferase SseK3
  • EC number
  • Short names
    Arginine GlcNAcyltransferase SseK3
  • Alternative names
    • Salmonella secreted effector K3

Gene names

    • Name
      sseK3
    • Ordered locus names
      SL1344_1928

Organism names

Accessions

  • Primary accession
    P0DUJ7

Proteomes

Subcellular Location

Secreted
Host Golgi apparatus
Note: Secreted via type III secretion system 2 (SPI-2 T3SS) (PubMed:21445262).
Localizes to host Golgi apparatus via lipid-binding (PubMed:32504010).

Keywords

Phenotypes & Variants

Disruption phenotype

Decreased apoptosis in infected macrophages, characterized by reduced CASP3, CASP8 ans CASP9 caspase activity.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis51Strongly reduced protein-arginine N-acetylglucosaminyltransferase activity, while retaining ability to inhibit the NF-kappa-B signaling.
Mutagenesis52Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis87-89Abolished localization to the host Golgi apparatus; when associated with A-234.
Mutagenesis153In 4RA; abolished auto-GlcNAcylation and reduced activity toward death domain-containing host target proteins; when associated with A-184, A-305 and A-335.
Mutagenesis184In 4RA; abolished auto-GlcNAcylation and reduced activity toward death domain-containing host target proteins; when associated with A-153, A-305 and A-335.
Mutagenesis224Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis226-228Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis234Abolished localization to the host Golgi apparatus; when associated with 87-A-A-89.
Mutagenesis247Does not affect protein-arginine N-acetylglucosaminyltransferase activity, while retaining ability to inhibit the NF-kappa-B signaling.
Mutagenesis251Does not affect protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis258Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis259Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis305In 4RA; abolished auto-GlcNAcylation and reduced activity toward death domain-containing host target proteins; when associated with A-153, A-184 and A-335.
Mutagenesis334Abolished protein-arginine N-acetylglucosaminyltransferase activity.
Mutagenesis335Does not affect protein-arginine N-acetylglucosaminyltransferase activity, but impairs the GlcNAcylation pattern of host target proteins. In 4RA; abolished auto-GlcNAcylation and reduced activity toward death domain-containing host target proteins; when associated with A-153, A-184 and A-305.

Miscellaneous

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004526011-335Protein-arginine N-acetylglucosaminyltransferase SseK3
Glycosylation153N-beta-linked (GlcNAc) arginine; by autocatalysis
Glycosylation184N-beta-linked (GlcNAc) arginine; by autocatalysis
Glycosylation305N-beta-linked (GlcNAc) arginine; by autocatalysis
Glycosylation335N-beta-linked (GlcNAc) arginine; by autocatalysis

Post-translational modification

Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins.

Keywords

PTM databases

Interaction

Subunit

Interacts with host TRIM32; without mediating its GlcNAcylation.

Protein-protein interaction databases

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif226-228DXD motif

Domain

Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product.

Sequence similarities

Belongs to the glycosyltransferase NleB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    335
  • Mass (Da)
    37,890
  • Last updated
    2021-06-02 v1
  • Checksum
    2BF80A0FC929E897
MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FQ312003
EMBL· GenBank· DDBJ
CBW18025.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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