LEXA_PSECP
ID LEXA_PSECP Reviewed; 249 AA.
AC B8HG97;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015};
DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015};
GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015}; OrderedLocusNames=Achl_1470;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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:0000255|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:0000255|HAMAP-Rule:MF_00015};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255|HAMAP-
CC Rule:MF_00015}.
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DR EMBL; CP001341; ACL39459.1; -; Genomic_DNA.
DR RefSeq; WP_015936681.1; NC_011886.1.
DR AlphaFoldDB; B8HG97; -.
DR SMR; B8HG97; -.
DR STRING; 452863.Achl_1470; -.
DR MEROPS; S24.001; -.
DR EnsemblBacteria; ACL39459; ACL39459; Achl_1470.
DR KEGG; ach:Achl_1470; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_0_11; -.
DR OMA; HVWLLPH; -.
DR OrthoDB; 1933795at2; -.
DR Proteomes; UP000002505; 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 transcription, DNA-templated; 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; 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; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Hydrolase; Repressor; SOS response; Transcription;
KW Transcription regulation.
FT CHAIN 1..249
FT /note="LexA repressor"
FT /id="PRO_1000116594"
FT DNA_BIND 45..65
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 210
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 138..139
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 249 AA; 26379 MW; 493AC6D3522C5DE2 CRC64;
MAAAATGGRA TSQPKKTTKG LTPRQKKILE TIQRSVNVNG YPPSMREIGD TVGLASLSSV
THQLSQLEKL GYLRRDPKRP RAMEVLMPLT LDGGATGRTA RQAAEPAAAA APGITASVTE
LPTALDTAMV PLVGRIAAGG PILADQVVED VMPLPRQLVG QGELFMLKVA GDSMVDAAIC
DGDWVVVRRQ ADAANGDIVA ALLDDEATVK TFRQRDGHTW LLPQNTQYEP ILGDHATIMG
KVVSVLRSL