LEXA_MYCS2
ID LEXA_MYCS2 Reviewed; 243 AA.
AC A0QVY5; I7G7A4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
GN OrderedLocusNames=MSMEG_2740, MSMEI_2673;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK70187.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39141.1; -; Genomic_DNA.
DR RefSeq; WP_003894124.1; NZ_SIJM01000032.1.
DR RefSeq; YP_887073.1; NC_008596.1.
DR AlphaFoldDB; A0QVY5; -.
DR SMR; A0QVY5; -.
DR STRING; 246196.MSMEI_2673; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; ABK70187; ABK70187; MSMEG_2740.
DR EnsemblBacteria; AFP39141; AFP39141; MSMEI_2673.
DR GeneID; 66734145; -.
DR KEGG; msg:MSMEI_2673; -.
DR KEGG; msm:MSMEG_2740; -.
DR PATRIC; fig|246196.19.peg.2708; -.
DR eggNOG; COG1974; Bacteria.
DR OMA; HVWLLPH; -.
DR OrthoDB; 1933795at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR CollecTF; EXPREG_00000170; -.
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: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..243
FT /note="LexA repressor"
FT /id="PRO_0000322745"
FT DNA_BIND 56..76
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 204
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 132..133
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 243 AA; 25778 MW; A9831462CD0D503A CRC64;
MSDDTGEFTD GSTESPADAD GAGRRRAVDN GLTERQRTIL EVIRASVTSR GYPPSIREIG
DAVGLTSTSS VAHQLRTLER KGYLRRDPNR PRAVDVRAAD DPAAAAVVTT DVAGSDALPE
PTFVPVLGRI AAGGPILAEE AVEDVFPLPR ELVGEGSLFL LKVVGDSMVD AAICDGDWVV
VRQQNVADNG DIVAAMIDGE ATVKTFKRAR GQVWLMPHNP AYDPIPGNEA AVLGKVVTVI
RKI
