D
IPR032674

LRR-containing bacterial E3 ligase, N-terminal

InterPro entry
Short nameLRR_E3_ligase_N

Description

This domain is found in the N terminus of a group of bacterium-specific E3 enzymes that function as type three secretion system (T3SS) effectors in Salmonella, Shigella, and other Gram-negative bacteria. It is approximately 50 amino acids in length. There are two completely conserved residues (Y and W) that may be functionally important. Proteins containing this domain include SspH1 from Salmonella typhimurium
[1]
and IpaH9.8 from Shigella flexneri
[2]
. The structure of the Shigella IpaH and Salmonella SspH1 has been solved
[3, 4]
.

References

1.Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Rohde JR, Breitkreutz A, Chenal A, Sansonetti PJ, Parsot C. Cell Host Microbe 1, 77-83, (2007). View articlePMID: 18005683

2.A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. Nat. Cell Biol. 12, 66-73; sup pp 1-9, (2010). View articlePMID: 20010814

3.Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Singer AU, Rohde JR, Lam R, Skarina T, Kagan O, Dileo R, Chirgadze NY, Cuff ME, Joachimiak A, Tyers M, Sansonetti PJ, Parsot C, Savchenko A. Nat. Struct. Mol. Biol. 15, 1293-301, (2008). View articlePMID: 18997778

4.Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Keszei AF, Tang X, McCormick C, Zeqiraj E, Rohde JR, Tyers M, Sicheri F. Mol. Cell. Biol. 34, 362-73, (2014). View articlePMID: 24248594

Cross References

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