ID C7HD61_CLOTM Unreviewed; 213 AA. AC C7HD61; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 33. DE RecName: Full=LexA repressor {ECO:0000256|HAMAP-Rule:MF_00015, ECO:0000256|RuleBase:RU003992}; DE EC=3.4.21.88 {ECO:0000256|HAMAP-Rule:MF_00015, ECO:0000256|RuleBase:RU003992}; GN Name=lexA {ECO:0000256|HAMAP-Rule:MF_00015}; GN ORFNames=ClothDRAFT_0726 {ECO:0000313|EMBL:EEU02426.1}; OS Ruminiclostridium thermocellum DSM 2360. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=572545 {ECO:0000313|EMBL:EEU02426.1}; RN [1] {ECO:0000313|EMBL:EEU02426.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2360 {ECO:0000313|EMBL:EEU02426.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Hemme C.L.; RT "The draft genome of Clostridium thermocellum DSM 2360."; RL Submitted (JUL-2009) 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. {ECO:0000256|HAMAP-Rule:MF_00015, CC ECO:0000256|SAAS:SAAS00031404}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor CC LexA. {ECO:0000256|HAMAP-Rule:MF_00015, CC ECO:0000256|SAAS:SAAS00079668}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00015, CC ECO:0000256|SAAS:SAAS00079540}. CC -!- SIMILARITY: Belongs to the peptidase S24 family. CC {ECO:0000256|HAMAP-Rule:MF_00015, ECO:0000256|RuleBase:RU003991}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEU02426.1}. 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; ACVX01000005; EEU02426.1; -; Genomic_DNA. DR ProteinModelPortal; C7HD61; -. DR EnsemblBacteria; EEU02426; EEU02426; ClothDRAFT_0726. DR PATRIC; 27272840; VBICloThe106508_0755. 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; SSF51306; SSF51306; 1. DR TIGRFAMs; TIGR00498; lexA; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|RuleBase:RU003991}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079534}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079563}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079549}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079638}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|RuleBase:RU003991, ECO:0000256|SAAS:SAAS00079615, KW ECO:0000313|EMBL:EEU02426.1}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079592}; KW SOS response {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079532}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079538}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00015, KW ECO:0000256|SAAS:SAAS00079530}. FT DNA_BIND 29 49 H-T-H motif. {ECO:0000256|HAMAP-Rule: FT MF_00015}. FT ACT_SITE 136 136 For autocatalytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_00015}. FT ACT_SITE 173 173 For autocatalytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_00015}. FT SITE 101 102 Cleavage; by autolysis. {ECO: FT 0000256|HAMAP-Rule:MF_00015}. SQ SEQUENCE 213 AA; 24031 MW; D1C4EE9AB8757C42 CRC64; MQNKINEKQQ KILDFLNEQI EKNGYPPSVR EICNAVGFKS TSTVHSYLEK LRKQGLIQKD PSKPRALKVI NNKKNSKTDE PKNIYSGKEL VEVPIIGKVT AGQPILAVEN IEDTFPLPLD FVQNSTVFML RVQGDSMIEA GIFDNDYIVV KQQSTANNGD IVVALIDDEA TVKTFYKEKG FIRLQPANKF YDPIIVRDNL SILGKVIGVF RKM //