ID E4TG52_CALNY Unreviewed; 206 AA. AC E4TG52; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=LexA repressor {ECO:0000256|HAMAP-Rule:MF_00015}; DE EC=3.4.21.88 {ECO:0000256|HAMAP-Rule:MF_00015}; GN Name=lexA {ECO:0000256|HAMAP-Rule:MF_00015}; GN OrderedLocusNames=Calni_0691 {ECO:0000313|EMBL:ADR18602.1}; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1). OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales; OC Calditerrivibrionaceae. OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18602.1, ECO:0000313|Proteomes:UP000007039}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Calditerrivibrio nitroreducens DSM RT 19672."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADR18602.1, ECO:0000313|Proteomes:UP000007039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1 RC {ECO:0000313|Proteomes:UP000007039}; RX PubMed=21475587; DOI=10.4056/sigs.1523807; RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Land M.; RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain RT (Yu37-1)."; RL Stand. Genomic Sci. 4:54-62(2011). CC -!- FUNCTION: Represses a number of genes involved in the response to DNA CC damage (SOS response), including recA and lexA. In the presence of CC single-stranded DNA, RecA interacts with LexA causing an autocatalytic CC cleavage which disrupts the DNA-binding part of LexA, leading to CC derepression of the SOS regulon and eventually DNA repair. CC {ECO:0000256|HAMAP-Rule:MF_00015}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00015}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00015}. CC -!- SIMILARITY: Belongs to the peptidase S24 family. CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|HAMAP-Rule:MF_00015, CC ECO:0000256|RuleBase:RU003991}. 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; CP002347; ADR18602.1; -; Genomic_DNA. DR RefSeq; WP_013450815.1; NC_014758.1. DR AlphaFoldDB; E4TG52; -. DR STRING; 768670.Calni_0691; -. DR MEROPS; S24.001; -. DR KEGG; cni:Calni_0691; -. DR eggNOG; COG1974; Bacteria. DR HOGENOM; CLU_066192_45_2_0; -. DR OrthoDB; 9787787at2; -. DR Proteomes; UP000007039; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule. DR CDD; cd06529; S24_LexA-like; 1. DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR HAMAP; MF_00015; LexA; 1. DR InterPro; IPR006200; LexA. DR InterPro; IPR039418; LexA-like. DR InterPro; IPR036286; LexA/Signal_pep-like_sf. DR InterPro; IPR006199; LexA_DNA-bd_dom. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR NCBIfam; TIGR00498; lexA; 1. DR PANTHER; PTHR33516; LEXA REPRESSOR; 1. DR PANTHER; PTHR33516:SF2; LEXA REPRESSOR; 1. DR Pfam; PF01726; LexA_DNA_bind; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR SUPFAM; SSF51306; LexA/Signal peptidase; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00015}; KW Reference proteome {ECO:0000313|Proteomes:UP000007039}; KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00015}; KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00015}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP- KW Rule:MF_00015}. FT DOMAIN 2..64 FT /note="LexA repressor DNA-binding" FT /evidence="ECO:0000259|Pfam:PF01726" FT DOMAIN 75..189 FT /note="Peptidase S24/S26A/S26B/S26C" FT /evidence="ECO:0000259|Pfam:PF00717" FT DNA_BIND 27..47 FT /note="H-T-H motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT ACT_SITE 117 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT ACT_SITE 154 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT SITE 82..83 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" SQ SEQUENCE 206 AA; 23394 MW; A54DD314E769234C CRC64; MDLTDRQKEC INFISRFIKD YGYPPTIQEI CNNLGIRSKN AGFKLLNALE SKGFIRRNRS ISRGIELLKI NNGIPILGRI TAGIPIDAEE NIEGYIPLED ILGDISGYFG LRVIGDSMVE KGILDGDIAI IKKQPDILNN QVGAFMINGE FTLKTFKMMD DGRIYLKPEN NKYKPIYITE NDTFEVVGLL KMVVRLFGED YEARKY //