ID   LEXA_MYCBP              Reviewed;         236 AA.
AC   A1KM58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=BCG_2733;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAL72721.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AM408590; CAL72721.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_019283510.1; NC_008769.1.
DR   AlphaFoldDB; A1KM58; -.
DR   SMR; A1KM58; -.
DR   MEROPS; S24.001; -.
DR   KEGG; mbb:BCG_2733; -.
DR   HOGENOM; CLU_066192_45_0_11; -.
DR   Proteomes; UP000001472; 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; Repressor; SOS response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..236
FT                   /note="LexA repressor"
FT                   /id="PRO_1000001304"
FT   DNA_BIND        51..71
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   ACT_SITE        197
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT   SITE            125..126
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   236 AA;  24813 MW;  8F9FE0D234A4A05F CRC64;
     MNDSNDTSVA GGAAGADSRV LSADSALTER QRTILDVIRA SVTSRGYPPS IREIGDAVGL
     TSTSSVAHQL RTLERKGYLR RDPNRPRAVN VRGADDAALP PVTEVAGSDA LPEPTFAPVL
     GRIAAGGPIL AEEAVEDVFP LPRELVGEGT LFLLKVIGDS MVEAAICDGD WVVVRQQNVA
     DNGDIVAAMI DGEATVKTFK RAGGQVWLMP HNPAFDPIPG NDATVLGKVV TVIRKV