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8  structures 1008  species 4  interactions 1166  sequences 6  architectures

Family: YopE (PF03545)

Summary: Yersinia virulence determinant (YopE)

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This is the Wikipedia entry entitled "YopE protein domain". More...

YopE protein domain Edit Wikipedia article

PDB 1hy5 EBI.jpg
crystal structure of the catalytic domain of yope-yersinia pestis gap effector protein.
Symbol YopE
Pfam PF03545
InterPro IPR014773
SCOP 1g4w

In molecular biology, the protein domain YopE refers to the secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior. It not only infects the host cell but also protects the bacteria. It undergoes several mechanisms to evade the hosts immune system. This particular protein domain can be referred to as a Rho GTPase-activating protein (GAP).


YopE is an effector protein of the bacteriaYersinia. It functions as a Rho GTPase-activating protein (GAP). YopE acts as both a virulence factor and a protective antigen. In order to evade detection by the host, YopE uses a number of different eukaryotic signalling pathways to counteract innate and adaptive immune responses of the host. YopE targets the small GTPases: RhoA, Rac1, and Rac2. YopE GAP activity inhibits two common methods of host immunity - phagocytosis and reactive oxygen species generation. Additionally, it is thought that YopE targets the following immune cells, in particular:

Evidence also suggests that CD8 T lymphocyte cells mediate protection against Yersinia by production of cytokines (e.g., tumor necrosis factor alpha [TNF-alpha] and gamma interferon [IFN]) and by killing bacteria-associated host cells to promote internalization by neighbouring phagocytes.[1][2]


Structurally speaking, YopE has 4 alpha helices arranged in a left handed Four-helical up-and-down bundle. This bundle acts as the GAP domain, because arginine from an alpha helix is inserted into a GTP-ase which catalyses GTP hydrolysis through stabilisation of the transition state.[3]


  1. ^ Rosqvist R, Forsberg A, Rimpiläinen M, Bergman T, Wolf-Watz H (April 1990). "The cytotoxic protein YopE of Yersinia obstructs the primary host defence". Mol. Microbiol. 4 (4): 657–67. doi:10.1111/j.1365-2958.1990.tb00635.x. PMID 2191183. 
  2. ^ Cheng LW, Schneewind O (July 1999). "Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells". J. Biol. Chem. 274 (31): 22102–8. doi:10.1074/jbc.274.31.22102. PMID 10419539. 
  3. ^ Stebbins CE, Galán JE (2000). "Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1.". Mol Cell 6 (6): 1449–60. PMID 11163217. 

This article incorporates text from the public domain Pfam and InterPro IPR014773

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Yersinia virulence determinant (YopE) Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR014773

Secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior. There have been four secretion systems described in animal enteropathogens, such as Salmonella and Yersinia, with further sequence similarities in plant pathogens like Ralstonia and Erwinia [PUBMED:9618447].

The type III secretion system is of great interest, as it is used to transport virulence factors from the pathogen directly into the host cell and is only triggered when the bacterium comes into close contact with the host. The protein subunits of the system are very similar to those of bacterial flagellar biosynthesis. However, while the latter forms a ring structure to allow secretion of flagellin and is an integral part of the flagellum itself [PUBMED:9618447], type III subunits in the outer membrane translocate secreted proteins through a channel-like structure.

Exotoxins secreted by the type III system do not possess a secretion signal, and are considered unique for this reason [PUBMED:9618447]. Yersinia secrete a Rho GTPase-activating protein, YopE [PUBMED:2307658, PUBMED:2191183], that disrupts the host cell actin cytoskeleton. YopE is regulated by another bacterial gene, SycE [PUBMED:10419539], that enables the exotoxin to remain soluble in the bacterial cytoplasm. A similar protein, exoenzyme S from Pseudomonas aeruginosa, has both ADP-ribosylation and GTPase activity [PUBMED:2191183, PUBMED:10419539].

Domain organisation

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Seed source: PRINTS
Previous IDs: Yers_vir_YopE;
Type: Family
Author: Griffiths-Jones SR
Number in seed: 4
Number in full: 1166
Average length of the domain: 69.80 aa
Average identity of full alignment: 60 %
Average coverage of the sequence by the domain: 14.57 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 37.6 37.1
Noise cut-off 21.0 20.1
Model length: 70
Family (HMM) version: 9
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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There are 4 interactions for this family. More...

YopE Ras YopE_N Y_phosphatase


For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the YopE domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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