ID   LEXA_CAUSK              Reviewed;         235 AA.
AC   B0SYZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=Caul_2782;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ71909.1; -; Genomic_DNA.
DR   RefSeq; YP_001684407.1; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 5900237; -.
DR   GenomeReviews; CP000927_GR; Caul_2782.
DR   KEGG; cak:Caul_2782; -.
DR   OMA; B0SYZ8; AILTFIR.
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    235       LexA repressor.
FT                                /FTId=PRO_1000074050.
FT   DNA_BIND     26     46       H-T-H motif (By similarity).
FT   ACT_SITE    156    156       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    193    193       For autocatalytic cleavage activity (By
FT                                similarity).
FT   SITE        121    122       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   235 AA;  25650 MW;  5686CC84E3A4BF22 CRC64;
     MLTRKQHELL MFIHERIKES GVSPSFDEMK EALDLASKSG IHRLITALEE RGFIRRLAHR
     ARALEVVKLP QQATTAAPPK GRGAFRPQVL EGGGQAPTTS AQPQMAADNS RELPILGRIA
     AGTPIDAIQH ERERLPVPES MLGAGEHYVL EVQGDSMIEA GILDGDYVII KKGDTANSGE
     IVVALVGEEA TLKRLRKKGG SIALEAANPK YETRIFGPDQ VEVQGKLVGL IRRYH
//