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Database: UniProt
Entry: U2D281_9FIRM
LinkDB: U2D281_9FIRM
Original site: U2D281_9FIRM 
ID   U2D281_9FIRM            Unreviewed;       206 AA.
AC   U2D281;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=HMPREF1547_01068 {ECO:0000313|EMBL:ERI96909.1};
OS   Blautia sp. KLE 1732.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1226324 {ECO:0000313|EMBL:ERI96909.1, ECO:0000313|Proteomes:UP000016485};
RN   [1] {ECO:0000313|EMBL:ERI96909.1, ECO:0000313|Proteomes:UP000016485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE 1732 {ECO:0000313|EMBL:ERI96909.1,
RC   ECO:0000313|Proteomes:UP000016485};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ERI96909.1}.
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DR   EMBL; AWSY01000039; ERI96909.1; -; Genomic_DNA.
DR   RefSeq; WP_015525162.1; NZ_KE993386.1.
DR   AlphaFoldDB; U2D281; -.
DR   PATRIC; fig|1226324.3.peg.995; -.
DR   HOGENOM; CLU_066192_45_1_9; -.
DR   OrthoDB; 9802364at2; -.
DR   Proteomes; UP000016485; 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; cd00090; HTH_ARSR; 1.
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; IPR011991; ArsR-like_HTH.
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   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          6..67
FT                   /note="LexA repressor DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01726"
FT   DOMAIN          86..199
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   206 AA;  23139 MW;  2B04A9D7EDC64244 CRC64;
     MTYGRISKKQ QEILDYMKNE ILNRGFPPSV REICEAVNLK STSSVHSHLE ALEKNGYIRR
     DATKPRAIEI IDDNFNLVRR EVVNVPLVGT VAAGQPILAV ENIDAYFPIP AEYMPNEQSF
     MLTVKGDSMI NAGIFDGDQV LVKQQATAEN GDMVVALIDD SATVKTFYKE NGYYRLQPEN
     DNMEPIIITG NLQILGKVFG VFRFFS
//
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