ID   DDROP_DEIDV             Reviewed;         129 AA.
AC   C1D3U5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=HTH-type transcriptional regulator DdrOP3 {ECO:0000305};
GN   Name=ddrOP3 {ECO:0000303|PubMed:25170972};
GN   OrderedLocusNames=Deide_3p02170 {ECO:0000312|EMBL:ACO48174.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG   Plasmid pDeide3.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115; PLASMID=pDeide3;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
RN   [2]
RP   CLEAVAGE.
RC   STRAIN=RD19;
RX   PubMed=25170972; DOI=10.1111/mmi.12774;
RA   Ludanyi M., Blanchard L., Dulermo R., Brandelet G., Bellanger L.,
RA   Pignol D., Lemaire D., de Groot A.;
RT   "Radiation response in Deinococcus deserti: IrrE is a metalloprotease that
RT   cleaves repressor protein DdrO.";
RL   Mol. Microbiol. 94:434-449(2014).
CC   -!- FUNCTION: Repressor specific for genes preceded by a
CC       radiation/desiccation response motif (RDRM) site, which is present
CC       upstream of several radiation-induced genes.
CC       {ECO:0000250|UniProtKB:C1CYP4}.
CC   -!- PTM: Cleaved between Leu-106 and Arg-107 by the IrrE metalloprotease
CC       after exposure to radiation. Cleavage inactivates DdrOP3, leading to
CC       derepression of the target genes. {ECO:0000305|PubMed:25170972}.
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DR   EMBL; CP001117; ACO48174.1; -; Genomic_DNA.
DR   RefSeq; WP_012695046.1; NC_012528.1.
DR   AlphaFoldDB; C1D3U5; -.
DR   SMR; C1D3U5; -.
DR   EnsemblBacteria; ACO48174; ACO48174; Deide_3p02170.
DR   KEGG; ddr:Deide_3p02170; -.
DR   HOGENOM; CLU_1924139_0_0_0; -.
DR   OrthoDB; 2063007at2; -.
DR   Proteomes; UP000002208; Plasmid pDeide3.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Plasmid; Reference proteome; Repressor; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..129
FT                   /note="HTH-type transcriptional regulator DdrOP3"
FT                   /id="PRO_0000432105"
FT   DOMAIN          7..61
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   SITE            106..107
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305|PubMed:25170972"
SQ   SEQUENCE   129 AA;  14612 MW;  54946D87245D7A09 CRC64;
     MKLCERLREL RQERGLRLKD IAGAAQISVP YLSDLERGRT NPSLETLQSL ASTYGITVHD
     LLEGVEFYGD QTAGALPQGL ADLIADPALG AQLTPDWIRT LARIELRGKR PRDKQDWFEI
     YLHLKRILD