ID N1ZAM4_9CLOT Unreviewed; 207 AA.
AC N1ZAM4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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 Synonyms=lexA_1 {ECO:0000313|EMBL:USF29879.1};
GN ORFNames=C820_001287 {ECO:0000313|EMBL:USF29879.1}, C820_02813
GN {ECO:0000313|EMBL:EMZ10840.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ10840.1};
RN [1] {ECO:0000313|EMBL:EMZ10840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ10840.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF29879.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF29879.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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. {ECO:0000256|HAMAP-
CC Rule:MF_00015}.
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DR EMBL; AQFQ01000030; EMZ10840.1; -; Genomic_DNA.
DR EMBL; CP097810; USF29879.1; -; Genomic_DNA.
DR AlphaFoldDB; N1ZAM4; -.
DR STRING; 97138.C820_02813; -.
DR PATRIC; fig|97138.3.peg.2813; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_1_9; -.
DR Proteomes; UP000012445; 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 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; 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 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|HAMAP-Rule:MF_00015};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00015};
KW DNA repair {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00015, ECO:0000313|EMBL:USF29879.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012445};
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 13..72
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 88..201
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT DNA_BIND 35..55
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 131
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 168
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 95..96
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 207 AA; 23450 MW; D0EB6E8EEBA92C76 CRC64;
MIFIRETALK QKQKQKQILQ YLKSEVQKKG YPPSVREISI ALGIKSTSTV HFHLSKLEQQ
GYIRRDPSKP RAIEILDSQE QKENIEIPIV GTITAGTPIL AVENIEDTFP LPTSFFNDND
DLFMLRVKGE SMIEAGIFHR DLILVRQQSY AENGDIVVAL LGELATVKTY YKGKSKIRLQ
PENSSMAPIF VTDVKILGKV VGLFRKF
//
