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Database: UniProt
Entry: A0A239ZZ03_CLOCO
LinkDB: A0A239ZZ03_CLOCO
Original site: A0A239ZZ03_CLOCO 
ID   A0A239ZZ03_CLOCO        Unreviewed;       200 AA.
AC   A0A239ZZ03;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ECO:0000313|EMBL:SQB33327.1};
GN   Synonyms=lexA_1 {ECO:0000313|EMBL:STA92506.1};
GN   ORFNames=HMJ28_00975 {ECO:0000313|EMBL:NOH14971.1}, NCTC13028_00320
GN   {ECO:0000313|EMBL:SQB33327.1}, NCTC2909_01144
GN   {ECO:0000313|EMBL:STA92506.1}, SAMN05216497_104107
GN   {ECO:0000313|EMBL:SDL00806.1};
OS   Clostridium cochlearium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1494 {ECO:0000313|EMBL:SQB33327.1, ECO:0000313|Proteomes:UP000250223};
RN   [1] {ECO:0000313|EMBL:SDL00806.1, ECO:0000313|Proteomes:UP000198811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-C224 {ECO:0000313|EMBL:SDL00806.1,
RC   ECO:0000313|Proteomes:UP000198811};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000250223, ECO:0000313|Proteomes:UP000253892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13028 {ECO:0000313|EMBL:SQB33327.1,
RC   ECO:0000313|Proteomes:UP000250223}, and NCTC2909
RC   {ECO:0000313|EMBL:STA92506.1, ECO:0000313|Proteomes:UP000253892};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:NOH14971.1, ECO:0000313|Proteomes:UP000528432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGROS13 {ECO:0000313|EMBL:NOH14971.1,
RC   ECO:0000313|Proteomes:UP000528432};
RA   Gupta T.B., Jauregui R., Risson A.N., Brightwell G., Maclean P.;
RT   "Draft genome sequence of Clostridium cochlearium strain AGROS13 isolated
RT   from a sheep dairy farm in New Zealand.";
RL   Submitted (MAY-2020) 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}.
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DR   EMBL; JABFIF010000001; NOH14971.1; -; Genomic_DNA.
DR   EMBL; FNGL01000004; SDL00806.1; -; Genomic_DNA.
DR   EMBL; UAWC01000001; SQB33327.1; -; Genomic_DNA.
DR   EMBL; UFWH01000001; STA92506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239ZZ03; -.
DR   STRING; 1494.SAMN05216497_104107; -.
DR   OrthoDB; 9802364at2; -.
DR   Proteomes; UP000198811; Unassembled WGS sequence.
DR   Proteomes; UP000250223; Unassembled WGS sequence.
DR   Proteomes; UP000253892; Unassembled WGS sequence.
DR   Proteomes; UP000528432; 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..64
FT                   /note="LexA repressor DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01726"
FT   DOMAIN          81..194
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
FT   DNA_BIND        27..47
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   ACT_SITE        124
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   ACT_SITE        161
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   SITE            88..89
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   200 AA;  22722 MW;  5D9802A2BD892CC4 CRC64;
     MARENKQEAI YEFIKEQLRE KGYPPSVREI CNAVGLRSTS TVHGHLKRLE QKGVIRRDPT
     KPRAIEVLDH SIIKKEMIDI PVIGTVTAGK PILAVENIED NFPLPIDYVK SDNQLFMLKI
     KGDSMIDAGI MNGDMAIIEK TNSALNGEIV VALLDNEATI KRFFKEKDYI RLQPENKTME
     PIIVKQCEII GKIVGLYRKY
//
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