3.4.21.88: Repressor LexA
This is an abbreviated version!
For detailed information about Repressor LexA, go to the full flat file.
Word Map on EC 3.4.21.88
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3.4.21.88
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reca
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lambda
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phage
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single-stranded
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regulon
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umud
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prophage
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mitomycin
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dna-damaging
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damage-inducible
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colicins
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sos-induced
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coprotease
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uv-irradiated
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nalidixic
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autodigestion
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self-cleavage
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sula
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lexa-binding
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reca430
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lysogens
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reca-dependent
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lexa-regulated
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reca-mediated
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lexadef
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promoter-operator
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drug development
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translesion
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antirepressors
- 3.4.21.88
- reca
- lambda
- phage
-
single-stranded
-
regulon
- umud
- prophage
- mitomycin
-
dna-damaging
-
damage-inducible
- colicins
-
sos-induced
-
coprotease
-
uv-irradiated
-
nalidixic
-
autodigestion
-
self-cleavage
- sula
-
lexa-binding
-
reca430
-
lysogens
-
reca-dependent
-
lexa-regulated
-
reca-mediated
-
lexadef
-
promoter-operator
- drug development
-
translesion
-
antirepressors
Reaction
Hydrolysis of Ala84-/-Gly bond in repressor LexA =
Synonyms
Cg2114, LexA, LexA protein, LexA repressor, LexA transcriptional repressor, LexA1, lexA_1, MtLexA, SOS regulatory protein dinR
ECTree
3.4.21.88 Repressor LexAAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.4.21.88 - Repressor LexA
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
additional information
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LexA protein is the repressor, which, during normal bacterial growth downregulates its own expression
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RecA
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DNA repair -inducing treatments activate RecA, which inactivates LexA by a specific cleavage reaction, leading to derepression of the SOS regulon, RecA stimulates the transition of LexA from its noncleavable to its cleavable conformation
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RecA
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when RecA is bound to the ssDNA, it becomes an active catalyst for the cleavage of the transcriptional repressor LexA, lowering the level of LexA and relieving the repression of the genes required for the damage repair, including its own transcription and that of lexA
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RecA
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stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. Data indicate that the RecA filament predominately induces self-cleavage in one monomer of the LexA dimer and that the resulting LexALexA/CTD heterodimer is an inactive intermediate, exhibiting weaker DNA binding. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA
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