ID   LEXA_VERSI              Reviewed;         202 AA.
AC   P0DOW5;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=LexA repressor {ECO:0000303|PubMed:27489856};
DE            EC=3.4.21.88;
GN   Name=lexA {ECO:0000303|PubMed:27489856};
GN   ORFNames=VSP_04780 {ECO:0000303|PubMed:27489856};
OS   Verrucomicrobium spinosum (strain ATCC 43997 / DSM 4136 / JCM 18804 / IFAM
OS   1439).
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; Verrucomicrobium.
OX   NCBI_TaxID=240016;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43997 / DSM 4136 / JCM 18804 / IFAM 1439;
RA   Ward N.L., Wu M., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Gwinn-Giglio M., Kothari S.P., Madupu R., Nelson W.C.,
RA   Rosovitz M.J., Shrivastava S., Sullivan S., Haft D.H., Selengut J.D.,
RA   Creasy T., Zafar N., Davidsen T.M., Yang Q., Ganapaty A., Dimitrov G.,
RA   Sosa J., Toms B., Khouri H.;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=ATCC 43997 / DSM 4136 / JCM 18804 / IFAM 1439;
RX   PubMed=27489856; DOI=10.3389/fmolb.2016.00033;
RA   Erill I., Campoy S., Kilic S., Barbe J.;
RT   "The Verrucomicrobia LexA-binding motif: insights into the evolutionary
RT   dynamics of the SOS response.";
RL   Front. Mol. Biosci. 3:33-33(2016).
CC   -!- FUNCTION: Binds the consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some
CC       genes have a tandem consensus sequence, at high concentrations their
CC       binding is cooperative (PubMed:27489856). Binds to the promoters of a
CC       number of genes, including dinB, imuA, lexA, recA, recQ, splB and uvrA
CC       (PubMed:27489856). Represses a number of genes involved in the response
CC       to DNA damage (SOS response) (By similarity). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P31080,
CC       ECO:0000269|PubMed:27489856}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88;
CC         Evidence={ECO:0000250|UniProtKB:P31080};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:27489856}.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; ABIZ01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_009959117.1; NZ_ABIZ01000001.1.
DR   AlphaFoldDB; P0DOW5; -.
DR   SMR; P0DOW5; -.
DR   OrthoDB; 1933795at2; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 1.
DR   Gene3D; 1.10.10.10; -; 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; Repressor; SOS response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..202
FT                   /note="LexA repressor"
FT                   /id="PRO_0000438702"
FT   ACT_SITE        123
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31080"
FT   ACT_SITE        159
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31080"
FT   SITE            85..86
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P31080"
SQ   SEQUENCE   202 AA;  22718 MW;  42CEDA013AABBE98 CRC64;
     MLTERQQELL DFLRVYQRQQ GVMPSTRDIQ LHFGFASQTA AMSHLKALER KGVIRRLAGK
     ARAVVFPEVM ERETVDIPIF GLIPAGFTAD NPEHSDGNLT LDLRTMGLSP RSKPFALKVR
     GDSMTGAHII QGDYVILEQR DPRPKDIVAA LMDGETTLKR YLVDNGQPFL RAENPSYPDL
     IPARELMIQG VMVGLFRPYN GR