ID A0A927BMC4_STRGL Unreviewed; 265 AA. AC A0A927BMC4; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 24-JUL-2024, entry version 5. 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:MBD2829628.1}; GN ORFNames=ID875_18685 {ECO:0000313|EMBL:MBD2829628.1}; OS Streptomyces globisporus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1908 {ECO:0000313|EMBL:MBD2829628.1, ECO:0000313|Proteomes:UP000616788}; RN [1] {ECO:0000313|EMBL:MBD2829628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=QF2 {ECO:0000313|EMBL:MBD2829628.1}; RA Montano E.T., Nideffer J.F., Brumage L., Erb M., Derman A.I., Davis J.P., RA Estrada E., Fu S., Le D., Vuppala A., Tran C., Luterstein E., Lakkaraju S., RA Panchagnula S., Ren C., Doan J., Tran S., Soriano J., Fujita Y., Gutala P., RA Fujii Q., Lee M., Bui A., Villarreal C., Shing S.R., Kim S., Freeman D., RA Racha V., Ho A., Kumar P., Falah K., Dawson T., Enustun E., Prichard A., RA Gomez A., Khanna K., Trigg S., Fernandez L., Pogliano K., Pogliano J.; RT "Isolation and characterization of Streptomyces bacteriophages and RT Streptomyces strains encoding biosynthetic arsenals: Streptomyces strains RT and phages for antibiotic discovery."; RL PLoS ONE 0:0-0(2020). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBD2829628.1}. 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; JACWUS010000003; MBD2829628.1; -; Genomic_DNA. DR Proteomes; UP000616788; Unassembled WGS sequence. 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; IPR050077; LexA_repressor. 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 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 58..121 FT /note="LexA repressor DNA-binding" FT /evidence="ECO:0000259|Pfam:PF01726" FT DOMAIN 147..259 FT /note="Peptidase S24/S26A/S26B/S26C" FT /evidence="ECO:0000259|Pfam:PF00717" FT DNA_BIND 84..104 FT /note="H-T-H motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 114..142 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..140 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 189 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT ACT_SITE 226 FT /note="For autocatalytic cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" FT SITE 154..155 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015" SQ SEQUENCE 265 AA; 28721 MW; 126D6DA3A309EDF3 CRC64; MTTTADSATI TARDHRSQSR LEPVHAMNDA LTNADGPDPA RSGRSMPGRP PGIRADSSGL TDRQRRVIEV IRDSVQRRGY PPSMREIGQA VGLSSTSSVA HQLMALERKG FLRRDPHRPR AYEVRGSDQP STQPTDTTGK PAASYVPLVG RIAAGGPILA EESVEDVFPL PRQLVGDGEL FVLKVVGDSM IEAAICDGDW VTVRRQPVAE NGDIVAAMLD GEATVKRFRR EDGHVWLLPH NAAYQPIPGD EATILGKVVA VLRRV //