LEXA_BACSU
ID LEXA_BACSU Reviewed; 205 AA.
AC P31080;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015, ECO:0000303|PubMed:8969214};
DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015, ECO:0000269|PubMed:8969214};
DE AltName: Full=SOS regulatory protein DinR {ECO:0000303|PubMed:1657879};
GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015};
GN Synonyms=dinR {ECO:0000303|PubMed:1657879}; OrderedLocusNames=BSU17850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION BY DNA DAMAGE AND
RP COMPETENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=1657879; DOI=10.1128/jb.173.22.7084-7091.1991;
RA Raymond-Denise A., Guillen N.;
RT "Identification of dinR, a DNA damage-inducible regulator gene of Bacillus
RT subtilis.";
RL J. Bacteriol. 173:7084-7091(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PROTEOLYTIC CLEAVAGE, AND
RP DNA-BINDING.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=8969214; DOI=10.1074/jbc.271.52.33502;
RA Miller M.C., Resnick J.B., Smith B.T., Lovett C.M. Jr.;
RT "The Bacillus subtilis dinR gene codes for the analogue of Escherichia coli
RT LexA. Purification and characterization of the DinR protein.";
RL J. Biol. Chem. 271:33502-33508(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP DNA-BINDING SPECIFICITY, AND POSSIBLE DIMERIZATION.
RC STRAIN=YB886A;
RX PubMed=9555905; DOI=10.1128/jb.180.8.2201-2211.1998;
RA Winterling K.W., Chafin D., Hayes J.J., Sun J., Levine A.S., Yasbin R.E.,
RA Woodgate R.;
RT "The Bacillus subtilis DinR binding site: redefinition of the consensus
RT sequence.";
RL J. Bacteriol. 180:2201-2211(1998).
CC -!- FUNCTION: Represses dinA, dinB, dinC, recA genes and itself by binding
CC to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have
CC a tandem consensus sequence and their binding is cooperative
CC (PubMed:1657879, PubMed:8969214, PubMed:9555905). 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; autocleavage
CC is maximal at pH 11 in the absence of RecA and ssDNA (PubMed:8969214).
CC {ECO:0000269|PubMed:8969214, ECO:0000269|PubMed:9555905,
CC ECO:0000305|PubMed:1657879}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00015,
CC ECO:0000269|PubMed:8969214};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015,
CC ECO:0000305|PubMed:1657879, ECO:0000305|PubMed:9555905}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the entire cell cycle with at
CC least a threefold increase when cells develop competence.
CC {ECO:0000269|PubMed:1657879}.
CC -!- INDUCTION: By mitomycin, requires an intact dinR gene (PubMed:1657879).
CC An SOS-independent induction of dinR occurs during competence, does not
CC require an intact dinR gene (PubMed:1657879).
CC {ECO:0000269|PubMed:1657879}.
CC -!- PTM: Following treatment with mitomycin C protein levels begin to
CC decrease after a 5-min lag and do not return to their original levels
CC for at least 90 min. {ECO:0000269|PubMed:8969214}.
CC -!- DISRUPTION PHENOTYPE: 100-fold decrease in homologous recombination
CC efficiency. {ECO:0000269|PubMed:1657879}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255|HAMAP-
CC Rule:MF_00015}.
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DR EMBL; M64684; AAA22573.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13669.1; -; Genomic_DNA.
DR PIR; A41315; A41315.
DR RefSeq; NP_389668.1; NC_000964.3.
DR RefSeq; WP_003238209.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P31080; -.
DR SMR; P31080; -.
DR STRING; 224308.BSU17850; -.
DR MEROPS; S24.001; -.
DR PaxDb; P31080; -.
DR PRIDE; P31080; -.
DR EnsemblBacteria; CAB13669; CAB13669; BSU_17850.
DR GeneID; 939564; -.
DR KEGG; bsu:BSU17850; -.
DR PATRIC; fig|224308.179.peg.1946; -.
DR eggNOG; COG1974; Bacteria.
DR InParanoid; P31080; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; P31080; -.
DR BioCyc; BSUB:BSU17850-MON; -.
DR PRO; PR:P31080; -.
DR Proteomes; UP000001570; Chromosome.
DR CollecTF; EXPREG_00000a00; -.
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 transcription, DNA-templated; 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; 1.10.10.10; -; 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 Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR00498; lexA; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Hydrolase; Reference proteome; Repressor; SOS response;
KW Transcription; Transcription regulation.
FT CHAIN 1..205
FT /note="LexA repressor"
FT /id="PRO_0000170010"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 127
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015,
FT ECO:0000305|PubMed:8969214"
FT ACT_SITE 165
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015,
FT ECO:0000305|PubMed:8969214"
FT SITE 91..92
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:8969214"
SQ SEQUENCE 205 AA; 22849 MW; 68EA3EC2FD950B1B CRC64;
MTKLSKRQLD ILRFIKAEVK SKGYPPSVRE IGEAVGLASS STVHGHLARL ETKGLIRRDP
TKPRAIEILD EEVDIPQSQV VNVPVIGKVT AGSPITAVEN IEEYFPLPDR MVPPDEHVFM
LEIMGDSMID AGILDKDYVI VKQQNTANNG EIVVAMTEDD EATVKRFYKE DTHIRLQPEN
PTMEPIILQN VSILGKVIGV FRTVH
