ID   LEXA_BURCM              Reviewed;         215 AA.
AC   Q0BFL9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=Bamb_1496;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Represses a number of genes involved in the response to
CC       DNA damage (SOS response), including recA and lexA. In the
CC       presence of single-stranded DNA, recA interacts with lexA causing
CC       an autocatalytic cleavage which disrupts the DNA-binding part of
CC       lexA, leading to derepression of the SOS regulon and eventually
CC       DNA repair (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
CC       lexA.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
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DR   EMBL; CP000440; ABI87054.1; -; Genomic_DNA.
DR   RefSeq; YP_773388.1; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 4309580; -.
DR   GenomeReviews; CP000440_GR; Bamb_1496.
DR   KEGG; bam:Bamb_1496; -.
DR   NMPDR; fig|339670.3.peg.2954; -.
DR   OMA; Q0BFL9; KVIGVFR.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-d...; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   HAMAP; MF_00015; -; 1.
DR   InterPro; IPR006199; LexA_DNA_bd.
DR   InterPro; IPR006200; Pept_S24_LexA.
DR   InterPro; IPR006197; Peptidase_S24_LexA_cons-reg.
DR   InterPro; IPR019759; Peptidase_S24_S26_cons-reg.
DR   InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01726; LexA_DNA_bind; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   TIGRFAMs; TIGR00498; lexA; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Hydrolase; Repressor; SOS response;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    215       LexA repressor.
FT                                /FTId=PRO_1000001267.
FT   DNA_BIND     28     48       H-T-H motif (By similarity).
FT   ACT_SITE    133    133       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    170    170       For autocatalytic cleavage activity (By
FT                                similarity).
FT   SITE         98     99       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   215 AA;  23208 MW;  2EEB9A3EAA00B154 CRC64;
     MTKLTARQQQ VFDLIRRAIE RSGFPPTRAE IAAELGFSSP NAAEEHLRAL ARKGVIELAA
     GASRGIRLLG IEDAPHQFTL PHAGLMQLSL PLVGRVAAGS PILAQEHISQ HYACDPALFT
     SKPDYLLKVR GLSMRDAGIL DGDLLAVQKR TEAKDGQIIV ARLGDDVTVK RLMRRPGGLE
     LIAENPDYEN IFVKAGSAEF ALEGIAVGLI RSGEL
//