ID H9UC63_FERPD Unreviewed; 198 AA.
AC H9UC63;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Ferpe_0997 {ECO:0000313|EMBL:AFG35106.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG35106.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00015}.
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DR EMBL; CP003260; AFG35106.1; -; Genomic_DNA.
DR RefSeq; WP_014451547.1; NC_017095.1.
DR AlphaFoldDB; H9UC63; -.
DR STRING; 771875.Ferpe_0997; -.
DR MEROPS; S24.001; -.
DR KEGG; fpe:Ferpe_0997; -.
DR PATRIC; fig|771875.3.peg.1022; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_1_0; -.
DR OrthoDB; 9802364at2; -.
DR Proteomes; UP000007384; 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; 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 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 1..61
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 77..191
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT ACT_SITE 119
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 156
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 83..84
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 198 AA; 22827 MW; C6111D2B640CD287 CRC64;
MRELTERQRR IYEFIKEYIT IKGYAPSIRD VARHFKMTPR GAQQHIIALE KKGYIKRSKG
ARAITLADRK ESIVVPVKGK IAAGQAIEMF EEVDEEIEVP IEMLRGYGEY FALKVQGDSM
TNAHIIDGDY VILKKQYTAE NNSIVAAVID DKITLKRFIL KDNLVELVPE NESYPIMRYE
PKKVRIIGKM VGLIRIIR
//
