IRRE_DEIRA
ID IRRE_DEIRA Reviewed; 328 AA.
AC Q9RXY7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Radiation response metalloprotease IrrE {ECO:0000250|UniProtKB:C1CZ84};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:C1CZ84};
DE AltName: Full=DNA repair regulatory protein IrrE {ECO:0000305};
DE AltName: Full=Inducer of pleiotropic protein for DNA repair {ECO:0000303|PubMed:12804570};
GN Name=irrE {ECO:0000303|PubMed:12399492};
GN Synonyms=pprI {ECO:0000303|PubMed:12804570};
GN OrderedLocusNames=DR_0167 {ECO:0000312|EMBL:AAF09762.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=12399492; DOI=10.1128/jb.184.22.6216-6224.2002;
RA Earl A.M., Mohundro M.M., Mian I.S., Battista J.R.;
RT "The IrrE protein of Deinococcus radiodurans R1 is a novel regulator of
RT recA expression.";
RL J. Bacteriol. 184:6216-6224(2002).
RN [3]
RP FUNCTION.
RX PubMed=12804570; DOI=10.1016/s0006-291x(03)00965-3;
RA Hua Y., Narumi I., Gao G., Tian B., Satoh K., Kitayama S., Shen B.;
RT "PprI: a general switch responsible for extreme radioresistance of
RT Deinococcus radiodurans.";
RL Biochem. Biophys. Res. Commun. 306:354-360(2003).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=22051194; DOI=10.1016/j.dnarep.2011.10.013;
RA Lu H., Chen H., Xu G., Shah A.M., Hua Y.;
RT "DNA binding is essential for PprI function in response to radiation damage
RT in Deinococcus radiodurans.";
RL DNA Repair 11:139-145(2012).
CC -!- FUNCTION: Plays a central regulatory role in DNA repair and protection
CC pathways in response to radiation stress (PubMed:12804570,
CC PubMed:22051194). Acts as a site-specific metalloprotease that cleaves
CC and inactivates the repressor protein DdrO, resulting in induced
CC expression of genes required for DNA repair and cell survival after
CC exposure to radiation (By similarity). Regulates the expression of
CC dozens of proteins from different pathways, including the important DNA
CC repair proteins RecA and PprA (PubMed:12399492, PubMed:12804570,
CC PubMed:22051194). Binds to the promoters of recA and pprA
CC (PubMed:22051194). {ECO:0000250|UniProtKB:C1CZ84,
CC ECO:0000269|PubMed:12399492, ECO:0000269|PubMed:12804570,
CC ECO:0000269|PubMed:22051194}.
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:0000250|UniProtKB:C1CZ84}.
CC -!- DISRUPTION PHENOTYPE: Mutant is sensitive to ionizing radiation, UV
CC light and mitomycin C. {ECO:0000269|PubMed:12399492}.
CC -!- CAUTION: It is uncertain whether Met-1 or Val-41 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF09762.1; -; Genomic_DNA.
DR PIR; G75551; G75551.
DR RefSeq; NP_293891.1; NC_001263.1.
DR RefSeq; WP_010886813.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RXY7; -.
DR SMR; Q9RXY7; -.
DR STRING; 243230.DR_0167; -.
DR EnsemblBacteria; AAF09762; AAF09762; DR_0167.
DR KEGG; dra:DR_0167; -.
DR PATRIC; fig|243230.17.peg.332; -.
DR eggNOG; COG2856; Bacteria.
DR HOGENOM; CLU_1052605_0_0_0; -.
DR OMA; ETLCNVG; -.
DR OrthoDB; 1840229at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 DNA-binding; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Stress response; Zinc.
FT CHAIN 1..328
FT /note="Radiation response metalloprotease IrrE"
FT /id="PRO_0000432103"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /evidence="ECO:0000250|UniProtKB:C1CZ84"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:C1CZ84"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:C1CZ84"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:C1CZ84"
SQ SEQUENCE 328 AA; 34757 MW; C6EEF587DE190317 CRC64;
MPSANVSPPC PSGVRGGGMG PKAKAEASKP HPQIPVKLPF VTAPDALAAA KARMRDLAAA
YVAALPGRDT HSLMAGVPGV DLKFMPLGWR DGAFDPEHNV ILINSAARPE RQRFTLAHEI
GHAILLGDDD LLSDIHDAYE GERLEQVIET LCNVAAAAIL MPEPVIAEML ERFGPTGRAL
AELAKRAEVS ASSALYALTE QTPVPVIYAV CAPGKPPREQ AASDEDAGPS TEKVLTVRAS
SSTRGVKYTL ASGTPVPADH PAALALATGM EVREESYVPF RSGRKMKAEV DAYPSRGIVA
VSFEFDPARL GRKDSEQADR DEPQDAAQ
