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Radiation response metalloprotease IrrE (EC 3.4.24.-) (DNA repair regulatory protein IrrE)

 IRRE_DEIDV              Reviewed;         281 AA.
C1CZ84; B5B9W8;
04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
26-MAY-2009, sequence version 1.
07-JUN-2017, entry version 37.
RecName: Full=Radiation response metalloprotease IrrE {ECO:0000305};
EC=3.4.24.- {ECO:0000269|PubMed:25170972};
AltName: Full=DNA repair regulatory protein IrrE {ECO:0000305};
Name=irrE {ECO:0000303|PubMed:19150362};
OrderedLocusNames=Deide_03030 {ECO:0000312|EMBL:ACO45122.1};
Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923).
Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
Deinococcaceae; Deinococcus.
NCBI_TaxID=546414;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VCD115 / DSM 17065 / LMG 22923;
PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P.,
Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P.,
Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S.,
Achouak W., Armengaud J.;
"Alliance of proteomics and genomics to unravel the specificities of
Sahara bacterium Deinococcus deserti.";
PLoS Genet. 5:E1000434-E1000434(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, DISRUPTION PHENOTYPE, X-RAY
CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC, ACTIVE SITE,
AND MUTAGENESIS OF HIS-35; PHE-48; GLU-83; HIS-86; TYR-160; CYS-175
AND HIS-217.
STRAIN=VCD115 / DSM 17065 / LMG 22923;
PubMed=19150362; DOI=10.1016/j.jmb.2008.12.062;
Vujicic-Zagar A., Dulermo R., Le Gorrec M., Vannier F., Servant P.,
Sommer S., de Groot A., Serre L.;
"Crystal structure of the IrrE protein, a central regulator of DNA
damage repair in deinococcaceae.";
J. Mol. Biol. 386:704-716(2009).
[3]
FUNCTION, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF GLU-83, AND
ACTIVE SITE.
STRAIN=RD19;
PubMed=25170972; DOI=10.1111/mmi.12774;
Ludanyi M., Blanchard L., Dulermo R., Brandelet G., Bellanger L.,
Pignol D., Lemaire D., de Groot A.;
"Radiation response in Deinococcus deserti: IrrE is a metalloprotease
that cleaves repressor protein DdrO.";
Mol. Microbiol. 94:434-449(2014).
-!- FUNCTION: Plays a central regulatory role in DNA repair and
protection pathways in response to radiation stress. Acts as a
site-specific metalloprotease that cleaves and inactivates the
repressor proteins DdrOC and DdrOP3, resulting in induced
expression of genes required for DNA repair and cell survival
after exposure to radiation. {ECO:0000269|PubMed:25170972}.
-!- ENZYME REGULATION: Protease activity is inhibited by EDTA.
{ECO:0000269|PubMed:25170972}.
-!- SUBUNIT: Interacts with DdrOC. {ECO:0000269|PubMed:25170972}.
-!- DOMAIN: Composed of three structural domains: an N-terminal zinc-
peptidase domain, a central helix-turn-helix motif, and a C-
terminal GAF-type domain. {ECO:0000269|PubMed:19150362}.
-!- DISRUPTION PHENOTYPE: Deletion mutant is radiosensitive.
{ECO:0000269|PubMed:19150362}.
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EMBL; CP001114; ACO45122.1; -; Genomic_DNA.
EMBL; FM200036; CAQ86664.1; -; mRNA.
PDB; 3DTE; X-ray; 2.60 A; A=1-281.
PDB; 3DTI; X-ray; 3.50 A; A=1-281.
PDB; 3DTK; X-ray; 3.24 A; A=1-281.
PDBsum; 3DTE; -.
PDBsum; 3DTI; -.
PDBsum; 3DTK; -.
SMR; C1CZ84; -.
STRING; 546414.Deide_03030; -.
MEROPS; M78.002; -.
PaxDb; C1CZ84; -.
EnsemblBacteria; ACO45122; ACO45122; Deide_03030.
KEGG; ddr:Deide_03030; -.
eggNOG; ENOG4105M03; Bacteria.
eggNOG; ENOG4111UPP; LUCA.
HOGENOM; HOG000072589; -.
OMA; ETLCNVG; -.
OrthoDB; POG091H04D9; -.
Proteomes; UP000002208; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
InterPro; IPR010359; IrrE_HExxH.
Pfam; PF06114; Peptidase_M78; 1.
PROSITE; PS00356; HTH_LACI_1; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Stress response; Zinc.
CHAIN 1 281 Radiation response metalloprotease IrrE.
/FTId=PRO_0000432102.
ACT_SITE 83 83 {ECO:0000305|PubMed:19150362,
ECO:0000305|PubMed:25170972}.
METAL 82 82 Zinc; catalytic.
{ECO:0000269|PubMed:19150362}.
METAL 86 86 Zinc; catalytic.
{ECO:0000269|PubMed:19150362}.
METAL 113 113 Zinc; catalytic.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 35 35 H->A: No change in radiotolerance; when
associated with A-48.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 48 48 F->A: No change in radiotolerance; when
associated with A-35.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 83 83 E->Q: Radiosensitive. Lack of protease
activity. {ECO:0000269|PubMed:19150362,
ECO:0000269|PubMed:25170972}.
MUTAGEN 86 86 H->S: Radiosensitive.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 160 160 Y->A: Decrease in radiotolerance.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 175 175 C->A: No change in radiotolerance.
{ECO:0000269|PubMed:19150362}.
MUTAGEN 217 217 H->L: Strong decrease in radiotolerance.
{ECO:0000269|PubMed:19150362}.
HELIX 10 27 {ECO:0000244|PDB:3DTE}.
STRAND 29 32 {ECO:0000244|PDB:3DTE}.
HELIX 34 39 {ECO:0000244|PDB:3DTE}.
STRAND 45 49 {ECO:0000244|PDB:3DTE}.
STRAND 56 59 {ECO:0000244|PDB:3DTE}.
TURN 60 63 {ECO:0000244|PDB:3DTE}.
STRAND 64 68 {ECO:0000244|PDB:3DTE}.
HELIX 73 91 {ECO:0000244|PDB:3DTE}.
HELIX 93 102 {ECO:0000244|PDB:3DTE}.
HELIX 105 124 {ECO:0000244|PDB:3DTE}.
HELIX 127 137 {ECO:0000244|PDB:3DTE}.
HELIX 141 151 {ECO:0000244|PDB:3DTE}.
HELIX 155 164 {ECO:0000244|PDB:3DTE}.
STRAND 170 177 {ECO:0000244|PDB:3DTE}.
STRAND 192 199 {ECO:0000244|PDB:3DTE}.
HELIX 218 225 {ECO:0000244|PDB:3DTE}.
STRAND 229 236 {ECO:0000244|PDB:3DTE}.
STRAND 242 251 {ECO:0000244|PDB:3DTE}.
STRAND 253 261 {ECO:0000244|PDB:3DTE}.
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


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