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Database: UniProt
Entry: R5D9M4_9FIRM
LinkDB: R5D9M4_9FIRM
Original site: R5D9M4_9FIRM 
ID   R5D9M4_9FIRM            Unreviewed;       205 AA.
AC   R5D9M4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ORFNames=BN457_01486 {ECO:0000313|EMBL:CCX73517.1};
OS   Dorea sp. CAG:105.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1262872 {ECO:0000313|EMBL:CCX73517.1, ECO:0000313|Proteomes:UP000017921};
RN   [1] {ECO:0000313|EMBL:CCX73517.1, ECO:0000313|Proteomes:UP000017921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:105 {ECO:0000313|Proteomes:UP000017921};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- 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:CCX73517.1}.
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DR   EMBL; CAWY010000018; CCX73517.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5D9M4; -.
DR   STRING; 1262872.BN457_01486; -.
DR   Proteomes; UP000017921; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000017921};
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          5..67
FT                   /note="LexA repressor DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01726"
FT   DOMAIN          86..198
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
FT   DNA_BIND        30..50
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   ACT_SITE        128
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   ACT_SITE        165
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   SITE            93..94
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   205 AA;  23104 MW;  7A70D3BFBB391E76 CRC64;
     MAQGKISAKQ QEILDYIKSQ ILERGFPPAV RDICEAVHLK STSSVHSHLE TLEKNGYIRR
     DSTKPRAIEI LDEAFNFTRR EMVNVPIVGR VAAGEPLLAE QNIEEYFPIP MEFMPNKQTF
     LLKVCGESMI NAGILNGDYV LAQEENTAHN GDMVVAMIED GATVKTFYKE EGVIRLQPEN
     DFMDPIIVPD CTILGKVIGV FRFMR
//
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