Gene Ontology annotation based on Enzyme Commission mapping
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin.
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SlrP is an E3 ubiquitin ligase that ubiquitinates host thioredoxin and ubiquitin
"In vitro, SlrP was able to mediate ubiquitination of ubiquitin and thioredoxin."
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Cys-546 is essential for E3 ligase catalytic activity
"A Cys residue conserved in other effectors of the same family that also possess E3 ubiquitin ligase activity was essential for this catalytic function."
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SlrP expression decreases thioredoxin activity and increases host cell death
"Stable expression of SlrP in HeLa cells resulted in a significant decrease of thioredoxin activity and in an increase of cell death."
The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3.
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ERdj3 (DNAJB11) identified as a second host target of SlrP
"Here, we identified ERdj3, an endoplasmic reticulum lumenal chaperone of the Hsp40/DnaJ family, as a new target for SlrP."
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SlrP partially localizes to the host ER in transfected HeLa cells
"Confocal microscopy and subcellular fractionation demonstrated that, in transfected HeLa cells, SlrP was partially located in the endoplasmic reticulum."
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SlrP interferes with ERdj3 binding to denatured substrates
"The presence of SlrP interfered with the binding of ERdj3 to a denatured substrate."
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SlrP modulates two independent targets -- thioredoxin in cytosol and ERdj3 in ER
"these data suggest that the role of SlrP in the interaction between Salmonella and the host cell is exerted through the modulation of the function of two independent targets: thioredoxin in the cytosol, and ERdj3 in the endoplasmic reticulum."
Deep research report on slrP (Falcon/Edison Scientific Literature)
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SlrP is a Salmonella SPI-2-related novel-type LRR-NEL E3 ubiquitin ligase (HECT-like NEL catalytic domain plus N-terminal leucine-rich repeats for substrate selection) translocated into host cells by type III secretion; two characterized substrates are cytosolic thioredoxin (Trx-1) and the ER-luminal Hsp40 ERdj3 - both are ubiquitinated, suppressing their respective chaperone and antioxidant activities.
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SlrP partially localizes to the host endoplasmic reticulum after translocation, consistent with its dual cytosolic/ER substrate targeting; the dual host-target strategy lets a single effector dampen redox buffering (Trx-1) and ER quality control (ERdj3) simultaneously during infection.