ID A0A0G1W5W1_9BACT Unreviewed; 502 AA.
AC A0A0G1W5W1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=UY03_C0011G0045 {ECO:0000313|EMBL:KKU77695.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_64.
OC Bacteria.
OX NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU77695.1, ECO:0000313|Proteomes:UP000034132};
RN [1] {ECO:0000313|EMBL:KKU77695.1, ECO:0000313|Proteomes:UP000034132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000256|HAMAP-
CC Rule:MF_00015}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00015}.
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:KKU77695.1}.
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DR EMBL; LCOL01000011; KKU77695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1W5W1; -.
DR Proteomes; UP000034132; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
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; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00092; N6_MTASE; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00015};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KKU77695.1};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..62
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 77..194
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT DOMAIN 243..496
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT ACT_SITE 120
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 158
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 84..85
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 502 AA; 56508 MW; 987250F01C762140 CRC64;
MLTARQKQIK DFVTKIIKQK GIAPSEREVA RHFRISASTA HQHLETLKEK GYLQKDPRRA
RGIEVTEPNN EKLVLIPLLG YITAGQLQEA IETRETIAVP QSKLPFPSGN YYGLRVSGDS
MVGKNISDGD IALVKKQNTA KNGENVVALV DNTETTLKTF YKERGRIRLQ PANKNHEPII
VEKDTPFEIQ GIVVDVIGRE PPKYEVGNVS IQSTIQNKKL PLNKIILGDA IKELQKLPDN
SCDIVIADPP YNIGKDFGNN LDKRELTEYV RWCKSWINEC IRTMKPSGTM FIYGFSEILA
HLSVEIPLQK RWLIWYYTNK NVASLNFWQR SHEAIICAWK EKPVFNRDEV REPYTEGFLN
GAAGRMRKGT LGRFSSSGLE TVYKAHEGGA LPRDVIKIPA LAGGAGMIER WFLCKTCDGV
YEPRQLKNHD GHEILKHPTQ KPLELSKKLI KSAMPKKEGV VLVPFVGSGS ECVAAKELGQ
SYLGFEINPD YIKIAKRVIS SM
//
