LEXA1_PSEPK
ID LEXA1_PSEPK Reviewed; 202 AA.
AC P0A153; P37453; Q9EUU0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=LexA repressor 1 {ECO:0000255|HAMAP-Rule:MF_00015};
DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015};
GN Name=lexA1 {ECO:0000255|HAMAP-Rule:MF_00015}; Synonyms=lexA, lexA-1;
GN OrderedLocusNames=PP_2143;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67756.1; -; Genomic_DNA.
DR RefSeq; NP_744292.1; NC_002947.4.
DR RefSeq; WP_010953131.1; NC_002947.4.
DR AlphaFoldDB; P0A153; -.
DR SMR; P0A153; -.
DR STRING; 160488.PP_2143; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; AAN67756; AAN67756; PP_2143.
DR KEGG; ppu:PP_2143; -.
DR PATRIC; fig|160488.4.peg.2260; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_3_6; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; P0A153; -.
DR BioCyc; PPUT160488:G1G01-2284-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR CollecTF; EXPREG_00000710; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; EXP:CollecTF.
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..202
FT /note="LexA repressor 1"
FT /id="PRO_0000170069"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 123
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 160
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 88..89
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 202 AA; 22148 MW; EF43C178C97D0679 CRC64;
MLKLTPRQAE ILAFIKRCLE DNGFPPTRAE IAQELGFKSP NAAEEHLKAL ARKGAIEMTP
GASRGIRIPG LEAKAEEAGL PIIGRVAAGA PILAEQHIEQ SCNINPAFFH PQADYLLRVH
GMSMKDVGIF DGDLLAVHTC REARNGQIVV ARIGDEVTVK RFKREGSKVW LLAENPEFAP
IEVDLKEQEL VIEGLSVGVI RR
