LEXA_CERS4
ID LEXA_CERS4 Reviewed; 228 AA.
AC Q9ZFA4; Q3J4Y7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=RHOS4_05790;
GN ORFNames=RSP_1997;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10511537; DOI=10.1093/genetics/153.2.525;
RA Mackenzie C., Simmons A.E., Kaplan S.;
RT "Multiple chromosomes in bacteria. The yin and yang of trp gene
RT localization in Rhodobacter sphaeroides 2.4.1.";
RL Genetics 153:525-538(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=10954081; DOI=10.1007/pl00008696;
RA Tapias A., Campoy S., Barbe J.;
RT "Analysis of the expression of the Rhodobacter sphaeroides lexA gene.";
RL Mol. Gen. Genet. 263:957-965(2000).
RN [4]
RP DNA-BINDING SPECIFICITY.
RX PubMed=9663685; DOI=10.1046/j.1365-2958.1998.00860.x;
RA Fernandez de Henestrosa A.R., Rivera E., Tapias A., Barbe J.;
RT "Identification of the Rhodobacter sphaeroides SOS box.";
RL Mol. Microbiol. 28:991-1003(1998).
CC -!- FUNCTION: Represses a number of genes involved in the response to DNA
CC damage (SOS response), including recA and lexA. Has been shown to bind
CC to the direct repeat sequence 5'-GTT-N(7)-GTTC-3'. 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:0000269|PubMed:10954081}.
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; AF108766; AAD09122.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA78147.1; -; Genomic_DNA.
DR PIR; T46859; T46859.
DR RefSeq; WP_002719150.1; NZ_CP030271.1.
DR RefSeq; YP_352048.1; NC_007493.2.
DR AlphaFoldDB; Q9ZFA4; -.
DR SMR; Q9ZFA4; -.
DR STRING; 272943.RSP_1997; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; ABA78147; ABA78147; RSP_1997.
DR GeneID; 57469393; -.
DR KEGG; rsp:RSP_1997; -.
DR PATRIC; fig|272943.9.peg.886; -.
DR eggNOG; COG1974; Bacteria.
DR OMA; HVWLLPH; -.
DR PhylomeDB; Q9ZFA4; -.
DR Proteomes; UP000002703; Chromosome 1.
DR CollecTF; EXPREG_000017e0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
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; IEP:CollecTF.
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 1: Evidence at protein level;
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..228
FT /note="LexA repressor"
FT /id="PRO_0000170079"
FT DNA_BIND 26..46
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 149
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 187
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 113..114
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 228 AA; 24800 MW; F5FD3F9CF67BBCC2 CRC64;
MLTRKQMELL DFIKTRMDRD GVPPSFDEMK DALDLRSKSG IHRLITALEE RGFIRRLAHR
ARAIEIVKLP EAMERAGFSA RAAKAAAAPL PKGAVTVETA GALDLPLMGR IAAGLPIEAI
NGGPQSVTVP GMMLSGRGQH YALEVKGDSM IAAGINDGDI VVIREQQTAD NGDIVVALVA
DHEATLKRYR RRGGMIALEP ANDSYETQVY PEQMVKVQGR LVGLIRSY
