LEXA_BACC0
ID LEXA_BACC0 Reviewed; 206 AA.
AC B7JIC6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015};
DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015};
GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015};
GN OrderedLocusNames=BCAH820_3708;
OS Bacillus cereus (strain AH820).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00015};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255|HAMAP-
CC Rule:MF_00015}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001283; ACK87676.1; -; Genomic_DNA.
DR RefSeq; WP_000413738.1; NC_011773.1.
DR AlphaFoldDB; B7JIC6; -.
DR SMR; B7JIC6; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; ACK87676; ACK87676; BCAH820_3708.
DR GeneID; 59155806; -.
DR GeneID; 64202240; -.
DR GeneID; 67508337; -.
DR KEGG; bcu:BCAH820_3708; -.
DR HOGENOM; CLU_066192_45_1_9; -.
DR OMA; HVWLLPH; -.
DR Proteomes; UP000001363; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00090; HTH_ARSR; 1.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00015; LexA; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR006200; LexA.
DR InterPro; IPR039418; LexA-like.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR006199; LexA_DNA-bd_dom.
DR InterPro; IPR006197; Peptidase_S24_LexA.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR00498; lexA; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Hydrolase; Repressor; SOS response; Transcription;
KW Transcription regulation.
FT CHAIN 1..206
FT /note="LexA repressor"
FT /id="PRO_1000192764"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 128
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 166
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 92..93
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 206 AA; 22890 MW; CC4077E937DF8D09 CRC64;
MEKLTKRQQD ILDFIKLKVQ EKGYPPSVRE IGQAVGLASS STVHGHLSRL EEKGYIRRDP
TKPRAIEILG EDRMDTETQS VIQVPIVGKV TAGLPITAVE SVEEHFPLPA SIVAGADQVF
MLRISGDSMI EAGIFDGDLV VVRQQQSAYN GEIVVALTED NEATVKRFYK EKDHFRLQPE
NSSLEPIILK QVSVIGKVIG VYRDLH