ID   LEXA_PRORE              Reviewed;         205 AA.
AC   Q07267;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
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};
OS   Providencia rettgeri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29944 / DSM 4542 / CIP 103182 / JCM 1675 / LMG 3259 / NCTC
RC   11801 / 1163;
RX   PubMed=8502572; DOI=10.1093/nar/21.9.2256;
RA   Riera J., Barbe J.;
RT   "Sequence of the Providencia rettgeri lexA gene and its control region.";
RL   Nucleic Acids Res. 21:2256-2256(1993).
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.
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}.
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DR   EMBL; X70965; CAA50300.1; -; Genomic_DNA.
DR   PIR; S33693; S33693.
DR   RefSeq; WP_004915217.1; NZ_VEVM01000018.1.
DR   AlphaFoldDB; Q07267; -.
DR   SMR; Q07267; -.
DR   STRING; 1141663.OOC_19972; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 61415880; -.
DR   OMA; HVWLLPH; -.
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; cd06529; S24_LexA-like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00015; LexA; 1.
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..205
FT                   /note="LexA repressor"
FT                   /id="PRO_0000170066"
FT   DNA_BIND        28..48
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   ACT_SITE        122
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   ACT_SITE        159
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   SITE            87..88
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   205 AA;  22847 MW;  0C5AB7084C044698 CRC64;
     MKALTARQQQ VYDLVRDHIS QTGMPPTRAE IAASLGFRSP NAAEEHLKAL ARKGVIEIVS
     GASRGIRLLL EEETEDQGLP LIGRVAAGEP LLAQEHIESH YQVDPELFKP HADFLLRVNG
     MSMKDIGIMD GDLLAVHKTQ NVHNGQVVVA RIEDEVTVKR FKQQGNRVEL IAENPEFEPI
     VVDLRQQNFT IEGLAVGVIR NSDWY