LEXA_BRUA2
ID LEXA_BRUA2 Reviewed; 240 AA.
AC Q2YRR1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BAB1_1167;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2]
RP POSSIBLE ACTIVITY REGULATION.
RC STRAIN=2308;
RX PubMed=16816190; DOI=10.1128/jb.01994-05;
RA Roux C.M., Booth N.J., Bellaire B.H., Gee J.M., Roop R.M. II, Kovach M.E.,
RA Tsolis R.M., Elzer P.H., Ennis D.G.;
RT "RecA and RadA proteins of Brucella abortus do not perform overlapping
RT protective DNA repair functions following oxidative burst.";
RL J. Bacteriol. 188:5187-5195(2006).
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 -!- ACTIVITY REGULATION: May be constitutively autocleaved; RecA is
CC constitutively activated in this strain, leading to continuous
CC transcription of recA. {ECO:0000305|PubMed:16816190}.
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; AM040264; CAJ11123.1; -; Genomic_DNA.
DR RefSeq; WP_002964272.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YRR1; -.
DR SMR; Q2YRR1; -.
DR STRING; 359391.BAB1_1167; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; CAJ11123; CAJ11123; BAB1_1167.
DR GeneID; 45124520; -.
DR GeneID; 55590827; -.
DR KEGG; bmf:BAB1_1167; -.
DR PATRIC; fig|359391.11.peg.65; -.
DR HOGENOM; CLU_066192_45_2_5; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; Q2YRR1; -.
DR Proteomes; UP000002719; 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; Reference proteome; Repressor; SOS response;
KW Transcription; Transcription regulation.
FT CHAIN 1..240
FT /note="LexA repressor"
FT /id="PRO_1000001263"
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
