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LEXA_FIBSS
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   03-AUG-2022, entry version 31.
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; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; 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   STRING; 59374.Fisuc_2822; -.
DR   PRIDE; P0DN68; -.
DR   eggNOG; COG1974; Bacteria.
DR   OMA; HVWLLPH; -.
DR   OrthoDB; 1933795at2; -.
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 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   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..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
 
 
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