ID LEXA_OPITP Reviewed; 200 AA.
AC B1ZZZ4;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=LexA repressor;
DE EC=3.4.21.88;
GN Name=lexA {ECO:0000303|PubMed:27489856}; OrderedLocusNames=Oter_4056;
OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=452637;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX PubMed=21398538; DOI=10.1128/jb.00228-11;
RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT abundant inhabitant of rice paddy soil ecosystems.";
RL J. Bacteriol. 193:2367-2368(2011).
RN [2]
RP DNA-BINDING, SUBUNIT, AND FUNCTION.
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX PubMed=27489856; DOI=10.3389/fmolb.2016.00033;
RA Erill I., Campoy S., Kilic S., Barbe J.;
RT "The Verrucomicrobia LexA-binding motif: insights into the evolutionary
RT dynamics of the SOS response.";
RL Front. Mol. Biosci. 3:33-33(2016).
CC -!- FUNCTION: Binds a consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some genes
CC have a tandem consensus sequence and their binding is cooperative
CC (PubMed:27489856). Binds to the promoters of a number of genes,
CC including lexA and splB (PubMed:27489856). Represses a number of genes
CC involved in the response to DNA damage (SOS response).
CC {ECO:0000250|UniProtKB:P31080, ECO:0000269|PubMed:27489856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88;
CC Evidence={ECO:0000250|UniProtKB:P31080};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:27489856}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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; CP001032; ACB77330.1; -; Genomic_DNA.
DR RefSeq; WP_012376858.1; NC_010571.1.
DR AlphaFoldDB; B1ZZZ4; -.
DR SMR; B1ZZZ4; -.
DR STRING; 452637.Oter_4056; -.
DR MEROPS; S24.001; -.
DR KEGG; ote:Oter_4056; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_2_0; -.
DR OrthoDB; 9802364at2; -.
DR Proteomes; UP000007013; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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 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; 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 Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase;
KW Reference proteome; Repressor; SOS response; Transcription;
KW Transcription regulation.
FT CHAIN 1..200
FT /note="LexA repressor"
FT /id="PRO_0000438701"
FT ACT_SITE 121
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:P31080"
FT ACT_SITE 158
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:P31080"
FT SITE 83..84
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P31080"
SQ SEQUENCE 200 AA; 22421 MW; 42F1F95F7D31C4F3 CRC64;
MLTEKQEAIL DYIRSVQAQR GVPPSTREIQ RHFGYESQNA AMNHLRALAR KGQLHQVDGA
TWGLKVSEVQ GHFELPIYGT IPAGVPSMQE QQPKETITFD PAVFRLRRPE RLWGLEVHGD
SMIDAHILDG DIAVLERREA KPGDIVAALV DETTTTLKRL AYVKGKPVLK PENARYALIV
PKDRLEIQGV FVGLIGRAKR
//
