LEXA_BRUMB
ID LEXA_BRUMB Reviewed; 240 AA.
AC C0RJB4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BMEA_A1188;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) 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; CP001488; ACO00922.1; -; Genomic_DNA.
DR RefSeq; WP_002964272.1; NC_012441.1.
DR AlphaFoldDB; C0RJB4; -.
DR SMR; C0RJB4; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; ACO00922; ACO00922; BMEA_A1188.
DR GeneID; 45124520; -.
DR GeneID; 55590827; -.
DR KEGG; bmi:BMEA_A1188; -.
DR HOGENOM; CLU_066192_45_2_5; -.
DR OMA; HVWLLPH; -.
DR Proteomes; UP000001748; Chromosome I.
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..240
FT /note="LexA repressor"
FT /id="PRO_1000116598"
FT DNA_BIND 26..46
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 161
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 199
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 126..127
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 240 AA; 26070 MW; 40661DAC60C8C7A2 CRC64;
MLTRKQHELL LFIHERLKET GIPPSFDEMK EALDLASKSG IHRLITALEE RGFIRRLPNR
ARALEVLRLP DSIAPGLSPQ KKFAPSVIEG SLGKVASVQP VRPAPAPQNS EAPATVSVPV
MGRIAAGVPI SAIQNQTHML SLPPEMIGAG EHYALEVKGD SMIDAGIFDG DTVIIKRGDT
ANPGEIVVAL VDEEEATLKR FRREGASIAL EAANPAYETR IFGPDRVHVQ GKLVGLIRRY
