AC MF_00015; DC Protein; auto TR HAMAP; MF_00015; -; 1; level=0 XX Names: LexA XX ID LEXA DE RecName: Full=LexA repressor; DE EC=3.4.21.88; GN Name=lexA; XX case CC -!- FUNCTION: Represses a number of genes involved in the response to DNA CC damage (SOS response), including recA and lexA. Binds to the 16 bp CC palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- CC stranded DNA, RecA interacts with LexA causing an autocatalytic CC cleavage which disrupts the DNA-binding part of LexA, leading to CC derepression of the SOS regulon and eventually DNA repair. else CC -!- FUNCTION: Represses a number of genes involved in the response to DNA CC damage (SOS response), including recA and lexA. In the presence of CC single-stranded DNA, RecA interacts with LexA causing an autocatalytic CC cleavage which disrupts the DNA-binding part of LexA, leading to CC derepression of the SOS regulon and eventually DNA repair. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the peptidase S24 family. XX DR Pfam; PF01726; LexA_DNA_bind; 1; trigger=no DR Pfam; PF00717; Peptidase_S24; 1; trigger=no DR PRINTS; PR00726; LEXASERPTASE; 1; trigger=no DR NCBIfam; TIGR00498; LexA; 1; trigger=no XX KW Transcription KW Transcription regulation KW Repressor KW DNA-binding KW DNA damage KW Autocatalytic cleavage KW Hydrolase KW DNA replication KW DNA repair KW SOS response XX GO GO:0003677; F:DNA binding GO GO:0004252; F:serine-type endopeptidase activity GO GO:0006281; P:DNA repair GO GO:0006260; P:DNA replication GO GO:0045892; P:negative regulation of DNA-templated transcription GO GO:0006974; P:DNA damage response GO GO:0009432; P:SOS response XX FT From: LEXA_ECOLI (P0A7C2) FT DNA_BIND 28..48 FT /note="H-T-H motif" FT ACT_SITE 119 FT /note="For autocatalytic cleavage activity" FT Condition: S FT ACT_SITE 156 FT /note="For autocatalytic cleavage activity" FT Condition: K FT SITE 84..85 FT /note="Cleavage; by autolysis" FT Condition: A-G XX Size: 192-275; Related: None; Template: P31080; P0A7C2; Q9ZFA4; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in GEOSL, NOCFA, PSEPK, PSESM, XANAC, XANCP Plasmid: None Comments: None XX # Revision 1.45 2023/06/01 //