LEXA_ECOLI
ID LEXA_ECOLI Reviewed; 202 AA.
AC P0A7C2; P03033; Q2M6R1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 142.
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}; Synonyms=exrA, spr, tsl, umuA;
GN OrderedLocusNames=b4043, JW4003;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7013987; DOI=10.1016/0092-8674(81)90432-3;
RA Horii T., Ogawa T., Ogawa H.;
RT "Nucleotide sequence of the lexA gene of E. coli.";
RL Cell 23:689-697(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT LEXA3.
RC STRAIN=K12;
RX PubMed=6272195; DOI=10.1093/nar/9.16.4149;
RA Markham B.E., Little J.W., Mount D.W.;
RT "Nucleotide sequence of the lexA gene of Escherichia coli K-12.";
RL Nucleic Acids Res. 9:4149-4161(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
RX PubMed=2259342; DOI=10.1007/bf00315795;
RA Oertel-Buchheit P., Lamerichs R.M., Schnarr M., Granger-Schnarr M.;
RT "Genetic analysis of the LexA repressor: isolation and characterization of
RT LexA(Def) mutant proteins.";
RL Mol. Gen. Genet. 223:40-48(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=6261224; DOI=10.1093/nar/9.3.529;
RA Miki T., Ebina Y., Kishi F., Nakazawa A.;
RT "Organization of the lexA gene of Escherichia coli and nucleotide sequence
RT of the regulatory region.";
RL Nucleic Acids Res. 9:529-543(1981).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-202.
RC STRAIN=K12;
RA Lilley P.E., Dixon N.E.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
RX PubMed=7027255; DOI=10.1073/pnas.78.7.4199;
RA Little J.W., Mount D.W., Yanisch-Perron C.R.;
RT "Purified lexA protein is a repressor of the recA and lexA genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4199-4203(1981).
RN [10]
RP FUNCTION.
RX PubMed=7027256; DOI=10.1073/pnas.78.7.4204;
RA Brent R., Ptashne M.;
RT "Mechanism of action of the lexA gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4204-4208(1981).
RN [11]
RP ROLE IN HYDROXYUREA RESISTANCE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [12]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
RA Erental A., Sharon I., Engelberg-Kulka H.;
RT "Two programmed cell death systems in Escherichia coli: an apoptotic-like
RT death is inhibited by the mazEF-mediated death pathway.";
RL PLoS Biol. 10:E1001281-E1001281(2012).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=2780544; DOI=10.1073/pnas.86.18.6863;
RA Lamerichs R.M.J.N., Padilla A., Boelens R., Kaptein R., Ottleben G.,
RA Rueterjans H., Granger-Schnarr M., Oertel P., Schnarr M.;
RT "The amino-terminal domain of LexA repressor is alpha-helical but differs
RT from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6863-6867(1989).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=8076591; DOI=10.1002/j.1460-2075.1994.tb06709.x;
RA Fogh R.H., Ottleben G., Rueterjans H., Schnarr M., Boelens R., Kaptein R.;
RT "Solution structure of the LexA repressor DNA binding domain determined by
RT 1H NMR spectroscopy.";
RL EMBO J. 13:3936-3944(1994).
RN [15]
RP 3D-STRUCTURE MODELING.
RX PubMed=7784426; DOI=10.1002/prot.340210305;
RA Knegtel R.M.A., Fogh R.H., Ottleben G., Rueterjans H., Dumoulin P.,
RA Schnarr M., Boelens R., Kaptein R.;
RT "A model for the LexA repressor DNA complex.";
RL Proteins 21:226-236(1995).
CC -!- FUNCTION: Represses a number of genes involved in the response to DNA
CC damage (SOS response), including recA and lexA. Binds to the 16 bp
CC palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-
CC 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. Implicated
CC in hydroxy radical-mediated cell death induced by hydroxyurea treatment
CC (PubMed:20005847).The SOS response controls an apoptotic-like death
CC (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module)
CC in response to DNA damaging agents that is mediated by RecA and LexA
CC (PubMed:22412352). {ECO:0000255|HAMAP-Rule:MF_00015,
CC ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:22412352,
CC ECO:0000269|PubMed:7027255, ECO:0000269|PubMed:7027256}.
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.
CC -!- INTERACTION:
CC P0A7C2; P0A7C2: lexA; NbExp=2; IntAct=EBI-553416, EBI-553416;
CC P0A7C2; P0A7W1: rpsE; NbExp=2; IntAct=EBI-553416, EBI-543949;
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255|HAMAP-
CC Rule:MF_00015}.
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DR EMBL; J01643; AAA24067.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43137.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77013.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78045.1; -; Genomic_DNA.
DR EMBL; L02362; AAA24068.1; -; Genomic_DNA.
DR PIR; A90808; ILEC.
DR RefSeq; NP_418467.1; NC_000913.3.
DR RefSeq; WP_000646078.1; NZ_STEB01000022.1.
DR PDB; 1JHC; X-ray; 2.00 A; A=68-202.
DR PDB; 1JHE; X-ray; 2.50 A; A/B=68-202.
DR PDB; 1JHF; X-ray; 1.80 A; A/B=1-202.
DR PDB; 1JHH; X-ray; 2.10 A; A/B=1-202.
DR PDB; 1LEA; NMR; -; A=1-84.
DR PDB; 1LEB; NMR; -; A=1-84.
DR PDB; 3JSO; X-ray; 2.29 A; A/B=1-202.
DR PDB; 3JSP; X-ray; 2.90 A; A/B=1-202.
DR PDB; 3K3R; X-ray; 3.20 A; E/F=1-202.
DR PDBsum; 1JHC; -.
DR PDBsum; 1JHE; -.
DR PDBsum; 1JHF; -.
DR PDBsum; 1JHH; -.
DR PDBsum; 1LEA; -.
DR PDBsum; 1LEB; -.
DR PDBsum; 3JSO; -.
DR PDBsum; 3JSP; -.
DR PDBsum; 3K3R; -.
DR AlphaFoldDB; P0A7C2; -.
DR SMR; P0A7C2; -.
DR BioGRID; 4261718; 11.
DR BioGRID; 852838; 8.
DR DIP; DIP-51082N; -.
DR IntAct; P0A7C2; 11.
DR STRING; 511145.b4043; -.
DR ChEMBL; CHEMBL4630871; -.
DR MEROPS; S24.001; -.
DR jPOST; P0A7C2; -.
DR PaxDb; P0A7C2; -.
DR PRIDE; P0A7C2; -.
DR EnsemblBacteria; AAC77013; AAC77013; b4043.
DR EnsemblBacteria; BAE78045; BAE78045; BAE78045.
DR GeneID; 67415408; -.
DR GeneID; 948544; -.
DR KEGG; ecj:JW4003; -.
DR KEGG; eco:b4043; -.
DR PATRIC; fig|511145.12.peg.4160; -.
DR EchoBASE; EB0528; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_3_6; -.
DR InParanoid; P0A7C2; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; P0A7C2; -.
DR BioCyc; EcoCyc:PD00205; -.
DR BRENDA; 3.4.21.88; 2026.
DR EvolutionaryTrace; P0A7C2; -.
DR PRO; PR:P0A7C2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_000007a0; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoliWiki.
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; IMP:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
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 3D-structure; Autocatalytic cleavage; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Hydrolase; Reference proteome; Repressor;
KW SOS response; Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="LexA repressor"
FT /id="PRO_0000170031"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 119
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 156
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 84..85
FT /note="Cleavage; by autolysis"
FT VARIANT 85
FT /note="G -> D (in lexA3, resistant to cleavage. Increased
FT sensitivity to hydroxyurea)"
FT /evidence="ECO:0000269|PubMed:20005847,
FT ECO:0000269|PubMed:6272195"
FT HELIX 6..22
FT /evidence="ECO:0007829|PDB:1JHF"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1JHF"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1JHF"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1JHF"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1JHF"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3JSO"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1JHF"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1JHF"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:1JHF"
SQ SEQUENCE 202 AA; 22358 MW; 7E8816A32C19EE71 CRC64;
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL ARKGVIEIVS
GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV DPSLFKPNAD FLLRVSGMSM
KDIGIMDGDL LAVHKTQDVR NGQVVVARID DEVTVKRLKK QGNKVELLPE NSEFKPIVVD
LRQQSFTIEG LAVGVIRNGD WL
