IRRE_DEIDV
ID IRRE_DEIDV Reviewed; 281 AA.
AC C1CZ84; B5B9W8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Radiation response metalloprotease IrrE {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:25170972};
DE AltName: Full=DNA repair regulatory protein IrrE {ECO:0000305};
GN Name=irrE {ECO:0000303|PubMed:19150362};
GN OrderedLocusNames=Deide_03030 {ECO:0000312|EMBL:ACO45122.1};
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 NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, DISRUPTION PHENOTYPE, X-RAY
RP CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-35; PHE-48; GLU-83; HIS-86; TYR-160; CYS-175 AND
RP HIS-217.
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19150362; DOI=10.1016/j.jmb.2008.12.062;
RA Vujicic-Zagar A., Dulermo R., Le Gorrec M., Vannier F., Servant P.,
RA Sommer S., de Groot A., Serre L.;
RT "Crystal structure of the IrrE protein, a central regulator of DNA damage
RT repair in deinococcaceae.";
RL J. Mol. Biol. 386:704-716(2009).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, MUTAGENESIS OF GLU-83, AND ACTIVE
RP SITE.
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: Plays a central regulatory role in DNA repair and protection
CC pathways in response to radiation stress. Acts as a site-specific
CC metalloprotease that cleaves and inactivates the repressor proteins
CC DdrOC and DdrOP3, resulting in induced expression of genes required for
CC DNA repair and cell survival after exposure to radiation.
CC {ECO:0000269|PubMed:25170972}.
CC -!- ACTIVITY REGULATION: Protease activity is inhibited by EDTA.
CC {ECO:0000269|PubMed:25170972}.
CC -!- SUBUNIT: Interacts with DdrOC. {ECO:0000269|PubMed:25170972}.
CC -!- DOMAIN: Composed of three structural domains: an N-terminal zinc-
CC peptidase domain, a central helix-turn-helix motif, and a C-terminal
CC GAF-type domain. {ECO:0000269|PubMed:19150362}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is radiosensitive.
CC {ECO:0000269|PubMed:19150362}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001114; ACO45122.1; -; Genomic_DNA.
DR EMBL; FM200036; CAQ86664.1; -; mRNA.
DR PDB; 3DTE; X-ray; 2.60 A; A=1-281.
DR PDB; 3DTI; X-ray; 3.50 A; A=1-281.
DR PDB; 3DTK; X-ray; 3.24 A; A=1-281.
DR PDBsum; 3DTE; -.
DR PDBsum; 3DTI; -.
DR PDBsum; 3DTK; -.
DR AlphaFoldDB; C1CZ84; -.
DR SMR; C1CZ84; -.
DR STRING; 546414.Deide_03030; -.
DR MEROPS; M78.002; -.
DR PaxDb; C1CZ84; -.
DR EnsemblBacteria; ACO45122; ACO45122; Deide_03030.
DR KEGG; ddr:Deide_03030; -.
DR eggNOG; COG2856; Bacteria.
DR HOGENOM; CLU_1052605_0_0_0; -.
DR OMA; ETLCNVG; -.
DR Proteomes; UP000002208; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1030; -; 1.
DR InterPro; IPR044853; G3DSA:1.10.10.1030.
DR InterPro; IPR010359; IrrE_HExxH.
DR Pfam; PF06114; Peptidase_M78; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Stress response; Zinc.
FT CHAIN 1..281
FT /note="Radiation response metalloprotease IrrE"
FT /id="PRO_0000432102"
FT REGION 262..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000305|PubMed:19150362,
FT ECO:0000305|PubMed:25170972"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19150362"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19150362"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 35
FT /note="H->A: No change in radiotolerance; when associated
FT with A-48."
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 48
FT /note="F->A: No change in radiotolerance; when associated
FT with A-35."
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 83
FT /note="E->Q: Radiosensitive. Lack of protease activity."
FT /evidence="ECO:0000269|PubMed:19150362,
FT ECO:0000269|PubMed:25170972"
FT MUTAGEN 86
FT /note="H->S: Radiosensitive."
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 160
FT /note="Y->A: Decrease in radiotolerance."
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 175
FT /note="C->A: No change in radiotolerance."
FT /evidence="ECO:0000269|PubMed:19150362"
FT MUTAGEN 217
FT /note="H->L: Strong decrease in radiotolerance."
FT /evidence="ECO:0000269|PubMed:19150362"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3DTE"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:3DTE"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:3DTE"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:3DTE"
SQ SEQUENCE 281 AA; 30029 MW; 146D79DED1CCB1E6 CRC64;
MTDPAPPPTA LAAAKARMRE LAASYGAGLP GRDTHSLMHG LDGITLTFMP MGQRDGAYDP
EHHVILINSQ VRPERQRFTL AHEISHALLL GDDDLLSDLH DEYEGDRLEQ VIETLCNVGA
AALLMPAELI DDLLTRFGPT GRALAELARR ADVSATSALY ALAERTAPPV IYAVCALSRQ
EDEGEGGGAK ELTVRASSAS AGVKYSLSAG TPVPDDHPAA LALDTRLPLA QDSYVPFRSG
RRMPAYVDAF PERQRVLVSF ALPAGRSEPD ADKPEAPGDQ S
