ID E4NI30_KITSK Unreviewed; 289 AA.
AC E4NI30;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
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:BAJ31160.1};
GN OrderedLocusNames=KSE_53850 {ECO:0000313|EMBL:BAJ31160.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ31160.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ31160.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
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; AP010968; BAJ31160.1; -; Genomic_DNA.
DR AlphaFoldDB; E4NI30; -.
DR STRING; 452652.KSE_53850; -.
DR MEROPS; S24.001; -.
DR KEGG; ksk:KSE_53850; -.
DR PATRIC; fig|452652.3.peg.5383; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_45_0_11; -.
DR Proteomes; UP000007076; 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 Reference proteome {ECO:0000313|Proteomes:UP000007076};
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 83..145
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 171..283
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT DNA_BIND 108..128
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 250
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 178..179
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 289 AA; 31417 MW; 5BB24DB579EFC91B CRC64;
MEHQPDERVA AMSTPSATSV MHTAEAKTAI PVQERSARTT DQESLDQTMS RSQPIEETPL
GAPVPVARSL PGRPPGIRTD EAGLTERQRR VIEVIRDSVQ RRGYPPSMRE IGQAVGLSST
SSVAHQLMAL ERKGFLRRDP HRPRAYEVRG VEVARPTATE TSGRPSTSYV PLVGRIAAGG
PILAEQTVED VFPLPRQLVG EGELFALTVK GDSMVEAAIC DGDWVTVRKQ PVAENGDIVA
AMIDGEATVK RLKREDGKIW LMPHNAAYEP IPGDNATILG KVVAVLRRL
//
