ID LEXA_XYLFA Reviewed; 211 AA. AC Q9PH24; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 20-JAN-2016, entry version 101. DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015}; DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015}; GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015}; GN OrderedLocusNames=XF_0122; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., RA Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., RA Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., RA Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., RA Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., RA Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., RA Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., RA Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., RA Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., RA Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., RA Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., RA Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., RA de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., RA da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., RA da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). 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. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor CC LexA. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SIMILARITY: Belongs to the peptidase S24 family. CC {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF82935.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE003849; AAF82935.1; ALT_INIT; Genomic_DNA. DR PIR; H82846; H82846. DR RefSeq; WP_023906043.1; NC_002488.3. DR ProteinModelPortal; Q9PH24; -. DR SMR; Q9PH24; 88-210. DR STRING; 160492.XF0122; -. DR EnsemblBacteria; AAF82935; AAF82935; XF_0122. DR GeneID; 1125639; -. DR KEGG; xfa:XF0122; -. DR PATRIC; 24130142; VBIXylFas578_0128. DR eggNOG; ENOG4105DS7; Bacteria. DR eggNOG; COG1974; LUCA. DR KO; K01356; -. DR OMA; ITNHINA; -. DR OrthoDB; EOG6JHRHJ; -. DR Proteomes; UP000000812; Chromosome. DR CollecTF; EXPREG_000017c0; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR HAMAP; MF_00015; LexA; 1. DR InterPro; IPR006200; LexA. DR InterPro; IPR006199; LexA_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. 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; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Hydrolase; Reference proteome; KW Repressor; SOS response; Transcription; Transcription regulation. FT CHAIN 1 211 LexA repressor. FT /FTId=PRO_0000170113. FT DNA_BIND 27 47 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00015}. FT ACT_SITE 131 131 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT ACT_SITE 168 168 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT SITE 96 97 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_00015}. SQ SEQUENCE 211 AA; 23395 MW; 3BB6A0560AD62571 CRC64; MSLSDIQQAI LSLITNHINA DGVSPSQTEI ARAFGFKGVR AVQHHLDVLE QQGMIRRVPR QARGIRLKHL TEVDETALAL QSEDVLRLPV LGRVAAGQPI GADIGEGRVV LLDRVFFSPA PDYLLRVQGD SMRDEGIFDG DLIGVHRTQD AHSGQIVVAR IDDEITVKLL KISKDRIRLL PRNPDFAPIE VRSDQDFAIE GLYCGLLRPN R //