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Items: 9

1.

ElaD/SseL N-terminal domain

This entry represents the N-terminal helical domain found in a group of CE proteases from human pathogens, including ElaD from E.coli, SseL from Salmonella typhimurium and ShiCE from Shigella [1,2], which are dedicated deubiquitinases (DUBs), proteases that reverse the addition of ubiquitin to substrates, and effectively hijacks the host's ubiquitination processes [2]. This domain is structurally similar to VHS domains and it serves to localise the catalytic domain (Pfam:PF22102) through an additional Ub binding site [1]. [1]. 32109687. Modification of the host ubiquitome by bacterial enzymes. Berglund J, Gjondrekaj R, Verney E, Maupin-Furlow JA, Edelmann MJ;. Microbiol Res. 2020;235:126429. [2]. 27425412. The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases. Pruneda JN, Durkin CH, Geurink PP, Ovaa H, Santhanam B, Holden DW, Komander D;. Mol Cell. 2016;63:261-276. (from Pfam)

Date:
2024-10-16
Family Accession:
NF047098.1
Method:
HMM
2.

ElaD/SseL-like C-terminal

This entry represents the C-terminal catalytic domain from a group of CE proteases from human pathogens including ElaD from E.coli, SseL from Salmonella typhimurium and ShiCE from Shigella [1,2], which are dedicated deubiquitinases (DUBs), proteases that reverse the addition of ubiquitin to substrates, and effectively hijacks the host's ubiquitination processes [2]. Paper describing PDB structure 5haf. [1]. 27425412. The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases. Pruneda JN, Durkin CH, Geurink PP, Ovaa H, Santhanam B, Holden DW, Komander D;. Mol Cell. 2016;63:261-276. [2]. 32109687. Modification of the host ubiquitome by bacterial enzymes. Berglund J, Gjondrekaj R, Verney E, Maupin-Furlow JA, Edelmann MJ;. Microbiol Res. 2020;235:126429. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046590.1
Method:
HMM
3.

Ulp1 family isopeptidase

This family is found almost entirely in eukaryotes, but prokaryotic members such as the deubiquitinating protease ElaD of intestinal pathogenic strains of Escherichia coli.

GO Terms:
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
cysteine-type peptidase activity (GO:0008234)
Date:
2024-10-16
Family Accession:
NF014901.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.

deubiquitinase ElaD

ElaD from Escherichia coli, like its homolog SseL from Salmonella is a Ulp1 protease that removes ubiquitin or ubiquitin-like proteins from target proteins to which they have been covalent attached by isopeptide bonds. Most Ulp1 amily proteases are found in eukaryotics, and prokaryotic homologs like ElaD tend to be virulence factors.

Gene:
elaD
Date:
2021-12-23
Family Accession:
NBR015034
Method:
BlastRule
7.

ElaD/SseL family deubiquitinase

Specific cysteine protease which targets ubiquitin and ubiquitin-like proteins covalently bound to target proteins

Date:
2021-12-23
Family Accession:
NF008812.1
Method:
HMM
8.
new record, indexing in progress
Family Accession:
9.

deubiquitinase

deubiquitinase is a C79 family peptidase, such as Escherichia coli protease ElaD that can act as an efficient and specific deubiquitinating enzyme in vitro; contains active site dyad Cys-His

Date:
2021-09-08
Family Accession:
10013887
Method:
Sparcle
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