ID   DDROC_DEIDV             Reviewed;         129 AA.
AC   C1CYP4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=HTH-type transcriptional regulator DdrOC {ECO:0000305};
GN   Name=ddrOC {ECO:0000303|PubMed:25170972};
GN   OrderedLocusNames=Deide_20570 {ECO:0000312|EMBL:ACO47074.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
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;
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   FUNCTION, CLEAVAGE, AND SUBUNIT.
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:0000269|PubMed:25170972}.
CC   -!- SUBUNIT: Forms at least dimers. Interacts with IrrE.
CC       {ECO:0000269|PubMed:25170972}.
CC   -!- PTM: Cleaved between Leu-106 and Arg-107 by the IrrE metalloprotease
CC       after exposure to radiation. Cleavage inactivates DdrOC, leading to
CC       derepression of the target genes. {ECO:0000269|PubMed:25170972}.
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DR   EMBL; CP001114; ACO47074.1; -; Genomic_DNA.
DR   RefSeq; WP_012694195.1; NC_012526.1.
DR   PDB; 6RMQ; X-ray; 3.00 A; A/B=1-129.
DR   PDB; 6RNX; X-ray; 2.84 A; A/B=1-129.
DR   PDB; 6RNZ; X-ray; 1.35 A; A/B=1-66.
DR   PDB; 6RO6; X-ray; 1.41 A; A/B/C/D/E/F/G/H=73-129.
DR   PDBsum; 6RMQ; -.
DR   PDBsum; 6RNX; -.
DR   PDBsum; 6RNZ; -.
DR   PDBsum; 6RO6; -.
DR   AlphaFoldDB; C1CYP4; -.
DR   SMR; C1CYP4; -.
DR   STRING; 546414.Deide_20570; -.
DR   PaxDb; C1CYP4; -.
DR   EnsemblBacteria; ACO47074; ACO47074; Deide_20570.
DR   KEGG; ddr:Deide_20570; -.
DR   eggNOG; COG1396; Bacteria.
DR   HOGENOM; CLU_1924139_0_0_0; -.
DR   OMA; DWYEIYL; -.
DR   OrthoDB; 2063007at2; -.
DR   Proteomes; UP000002208; Chromosome.
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   Pfam; PF01381; HTH_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Repressor; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..129
FT                   /note="HTH-type transcriptional regulator DdrOC"
FT                   /id="PRO_0000432104"
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:0000269|PubMed:25170972"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:6RNZ"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:6RNZ"
FT   HELIX           29..36
FT                   /evidence="ECO:0007829|PDB:6RNZ"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:6RNZ"
FT   HELIX           58..62
FT                   /evidence="ECO:0007829|PDB:6RNZ"
FT   HELIX           78..85
FT                   /evidence="ECO:0007829|PDB:6RO6"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:6RO6"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:6RO6"
FT   HELIX           95..102
FT                   /evidence="ECO:0007829|PDB:6RO6"
FT   HELIX           114..127
FT                   /evidence="ECO:0007829|PDB:6RO6"
SQ   SEQUENCE   129 AA;  14737 MW;  48B69186ECF6FEA0 CRC64;
     MKLHERLREL RSERGLRLKD VAEVAQISVP YLSDLERGRT NPSLETLQTL AGAYNITVHD
     LLEGVEFYGA STEGALPKGL SDLIADPTLG PQITPDWVRT LSRIELRGKR PRDKQDWYEI
     YLHLKRILS