ID   LEXA_DELAS              Reviewed;         224 AA.
AC   A9BWH9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; OrderedLocusNames=Daci_3565;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) 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}.
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DR   EMBL; CP000884; ABX36199.1; -; Genomic_DNA.
DR   RefSeq; WP_012205399.1; NC_010002.1.
DR   AlphaFoldDB; A9BWH9; -.
DR   SMR; A9BWH9; -.
DR   STRING; 398578.Daci_3565; -.
DR   MEROPS; S24.001; -.
DR   PRIDE; A9BWH9; -.
DR   EnsemblBacteria; ABX36199; ABX36199; Daci_3565.
DR   GeneID; 60687774; -.
DR   KEGG; dac:Daci_3565; -.
DR   eggNOG; COG1974; Bacteria.
DR   HOGENOM; CLU_066192_45_3_4; -.
DR   OMA; HVWLLPH; -.
DR   Proteomes; UP000000784; 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; 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; Reference proteome; Repressor; SOS response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..224
FT                   /note="LexA repressor"
FT                   /id="PRO_1000089560"
FT   DNA_BIND        31..51
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   ACT_SITE        142
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   ACT_SITE        179
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   SITE            107..108
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   224 AA;  24217 MW;  68265B671A3B9AD4 CRC64;
     MLDHPKLTAR QQQILDLIQA AISRTGAPPT RAEIANTLGF KSANAAEEHL QALARKGVIE
     LVSGTSRGIR LRTDTVRNIN AARGTSFGLP LSALAPLMLP LVGRVAAGSP ILAQEHIDQT
     YSVEPSLFQT RPDYLLRVRG MSMRDAGIMD GDLLAVQSAH EARNGQIVVA RLGDEVTVKR
     LRRTTQGVEL LPENPDYPVI RVAPEEAFAI EGLAVGLIRN SMSM