ID LEXA_FIBSS Reviewed; 217 AA.
AC P0DN68;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=FSU_0077;
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=59374;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15528664; DOI=10.1099/mic.0.27315-0;
RA Mazon G., Erill I., Campoy S., Cortes P., Forano E., Barbe J.;
RT "Reconstruction of the evolutionary history of the LexA-binding sequence.";
RL Microbiology 150:3783-3795(2004).
CC -!- FUNCTION: Probably represses a number of genes involved in the response
CC to DNA damage (SOS response), including itself, recA, uvrA, ruvAB and
CC ssb (PubMed:15528664). The probable consensus LexA box is 5'-TGCAC-N4-
CC GTGCA-3' (PubMed:15528664). In the presence of single-stranded DNA,
CC RecA interacts with LexA causing an autocatalytic cleavage which
CC disrupts the DNA-binding part of LexA, leading to derepression of the
CC SOS regulon and eventually DNA repair (Probable).
CC {ECO:0000269|PubMed:15528664, ECO:0000305}.
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; CP002158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_015732425.1; NC_017448.1.
DR AlphaFoldDB; P0DN68; -.
DR SMR; P0DN68; -.
DR GeneID; 34754062; -.
DR eggNOG; COG1974; Bacteria.
DR OrthoDB; 9802364at2; -.
DR Proteomes; UP000000517; Chromosome.
DR CollecTF; EXPREG_000003b0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:CollecTF.
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 DNA-templated transcription; 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; 2.10.109.10; Umud Fragment, subunit A; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR00498; lexA; 1.
DR PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR PANTHER; PTHR33516:SF2; LEXA REPRESSOR; 1.
DR Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Hydrolase; Repressor; SOS response; Transcription;
KW Transcription regulation.
FT CHAIN 1..217
FT /note="LexA repressor"
FT /id="PRO_0000435132"
FT DNA_BIND 35..55
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 137
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 174
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 101..102
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 217 AA; 24288 MW; C831385424BD34FF CRC64;
MENTNEKRKE MTARQEEIYE YIKKYSKENH MPPTVREIGN HFDISSTNGV RSILAALIKK
GYINRSPRLS RGIEILSDDK ESSKEVASNT IEIPIVGRVA AGTPILAVQN LEGTVTIDRD
FLACRSDVFA LRVKGDSMIN AGIFDGDLIF ARQQKTADLG EIVVAQIDNE ATVKYYHPSA
DHVELRPANP KYKPIIVNNR KDFSIAGRVI GVMRKVN
//
