ID   LEXA_BURTA              Reviewed;         215 AA.
AC   Q2SVP7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=BTH_I2481;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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; CP000086; ABC37161.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_443002.1; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 3847935; -.
DR   GenomeReviews; CP000086_GR; BTH_I2481.
DR   KEGG; bte:BTH_I2481; -.
DR   TIGR; BTH_I2481; -.
DR   HOGENOM; Q2SVP7; -.
DR   BioCyc; BTHA271848:BTH_I2481-MON; -.
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_0000322717.
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;  23169 MW;  9BB608CC85384453 CRC64;
     MIKLTARQQQ VFDLIRRAIE RSGFPPTRAE IAAELGFSSP NAAEEHLRAL ARKGVIELAA
     GASRGIRLLG LDDAPHQLTL PHAALMQLSL PLVGRVAAGS PILAQEHISQ HYACDPALFS
     SKPDYLLKVR GLSMRDAGIL DGDLLAVQKR AEAKDGQIIV ARLGDDVTVK RLKRRPGGVE
     LIAENPDYEN IFVKAGSAEF ALEGIAVGLI RPGEF
//