ID LEXA_PARDP Reviewed; 232 AA. AC A1B3Z0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 11-JUL-2012, entry version 45. DE RecName: Full=LexA repressor; DE EC=3.4.21.88; GN Name=lexA; OrderedLocusNames=Pden_2142; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., RA van Spanning R.J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Paracoccus denitrificans RT PD1222."; RL Submitted (DEC-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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000489; ABL70234.1; -; Genomic_DNA. DR RefSeq; YP_915930.1; NC_008686.1. DR ProteinModelPortal; A1B3Z0; -. DR STRING; A1B3Z0; -. DR MEROPS; S24.001; -. DR GeneID; 4579959; -. DR GenomeReviews; CP000489_GR; Pden_2142. DR KEGG; pde:Pden_2142; -. DR PATRIC; 22855409; VBIParDen97112_2073. DR eggNOG; COG1974; -. DR HOGENOM; HOG000232168; -. DR KO; K01356; -. DR OMA; IHERIKE; -. DR ProtClustDB; PRK00215; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 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 HAMAP; MF_00015; LexA; 1; -. DR InterPro; IPR006199; LexA_DNA-bd_dom. DR InterPro; IPR006200; Pept_S24_LexA. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn. DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. DR Pfam; PF01726; LexA_DNA_bind; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR SUPFAM; SSF51306; Pept_S24_S26_C; 1. 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 1 232 LexA repressor. FT /FTId=PRO_1000001312. FT DNA_BIND 26 46 H-T-H motif (By similarity). FT ACT_SITE 153 153 For autocatalytic cleavage activity (By FT similarity). FT ACT_SITE 191 191 For autocatalytic cleavage activity (By FT similarity). FT SITE 117 118 Cleavage; by autolysis (By similarity). SQ SEQUENCE 232 AA; 25645 MW; 37A94476DF06FC62 CRC64; MLTRKQIQLL EFIQARMARD GVPPSFDEMK LALDLRSKSG IHRLVTALEE RGFIRRLPHR ARALEIVRLP ESLSKGPGFQ PRVIEGTMPD RPAPLPRGAM EVSVSAIELP VMGRIAAGVP IEAISEISHH IAVPTTMLSG QDRHYALEVR GDSMIEAGIN DGDVVVIREQ NAAESGDIVV ALVDGYEATL KRYRRKGNMI ALEAANPAYE TRVLPEDKVR IQGRLVGLIR SY //