ID LEXA_XYLFA STANDARD; PRT; 211 AA. AC Q9PH24; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-MAY-2005 (Rel. 47, Last annotation update) DE LexA repressor (EC 3.4.21.88). GN Name=lexA; OrderedLocusNames=Xf0122; OS Xylella fastidiosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=2371; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX MEDLINE=20365717; 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. Binds to the CC 16 bp palindromic sequence 5'-CTGT-AT(4)-ACAG-3'. In the presence CC of single-stranded DNA, recA interacts with lexA causing an CC 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; AE003865; AAF82935.1; ALT_INIT; Genomic_DNA. DR HSSP; P03033; 1JHF. DR MEROPS; S24.001; -. DR HAMAP; MF_00015; -; 1. DR InterPro; IPR006199; LexA_DNA_bind. DR InterPro; IPR006200; Pept_S24_LexA. DR InterPro; IPR006198; Pept_S24_S26. DR InterPro; IPR011056; Pept_S24_S26_C. DR InterPro; IPR006197; Pept_S24_SOS. DR InterPro; IPR009058; Wing_hlx_DNA_bnd. DR Pfam; PF01726; LexA_DNA_bind; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR TIGRFAMs; TIGR00498; lexA; 1. KW Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; KW Transcription; Transcription regulation. FT DNA_BIND 27 47 H-T-H motif (By similarity). FT ACT_SITE 131 131 Involved in auto-cleavage (By FT similarity). FT ACT_SITE 168 168 Involved in auto-cleavage (By FT similarity). FT SITE 96 97 Cleavage (auto-) (By similarity). 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 //