ID A0A8A6B398_9GAMM Unreviewed; 205 AA. AC A0A8A6B398; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. 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 ECO:0000313|EMBL:QTH65362.1}; GN ORFNames=J1N51_09785 {ECO:0000313|EMBL:QTH65362.1}; OS Psychrosphaera ytuae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Psychrosphaera. OX NCBI_TaxID=2820710 {ECO:0000313|EMBL:QTH65362.1}; RN [1] {ECO:0000313|EMBL:QTH65362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MTZ26 {ECO:0000313|EMBL:QTH65362.1}; RA Zhang J., Xu X.-D.; RT "Description of Psychrosphaera ytuae sp. nov. isolated from deep sea RT sediment of South China Sea."; RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases. 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; CP072110; QTH65362.1; -; Genomic_DNA. DR KEGG; psym:J1N51_09785; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEA:InterPro. DR CDD; cd06529; S24_LexA-like; 1. DR Gene3D; 1.10.10.10; -; 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 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 {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 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 1..65 FT /note="LexA_DNA_bind" FT /evidence="ECO:0000259|Pfam:PF01726" FT DOMAIN 80..195 FT /note="Peptidase_S24" FT /evidence="ECO:0000259|Pfam:PF00717" FT DNA_BIND 28..48 FT /note="H-T-H motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT ACT_SITE 122 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT ACT_SITE 159 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT SITE 87..88 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" SQ SEQUENCE 205 AA; 22425 MW; 849C63B5C9690E64 CRC64; MRPLTARQSE ILELIRDTII STGMPPTRAE IAKQLGFRSA NAAEDHLKAL AKKGFIEMLS GTSRGIRLTE EITEQDSGLP LIGKVAAGSP ILAMEHVDRH VNVDPLMFSP SADFLLKVEG ESMKDIGILD GDLLAVHKTQ TARDGQVVVA RVEDDVTVKR LERKGSQVIL HAENEEFSPI KVDLNYQEFA IEGLAVGVIR NSSLM //