ID PERR_CLOAB Reviewed; 138 AA.
AC Q97FU2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Transcriptional regulator PerR;
DE AltName: Full=Oxidative stress genes repressor;
GN Name=perR; OrderedLocusNames=CA_C2634;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP FUNCTION AS A REPRESSOR, DISRUPTION PHENOTYPE, AND ROLE IN OXIDATIVE STRESS
RP DEFENSE.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=18430081; DOI=10.1111/j.1365-2958.2008.06192.x;
RA Hillmann F., Fischer R.J., Saint-Prix F., Girbal L., Bahl H.;
RT "PerR acts as a switch for oxygen tolerance in the strict anaerobe
RT Clostridium acetobutylicum.";
RL Mol. Microbiol. 68:848-860(2008).
RN [3]
RP FUNCTION AS A PEROXIDE SENSOR, PERR REGULON, AND DNA-BINDING.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19648241; DOI=10.1128/jb.00351-09;
RA Hillmann F., Doring C., Riebe O., Ehrenreich A., Fischer R.J., Bahl H.;
RT "The role of PerR in O2-affected gene expression of Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 191:6082-6093(2009).
CC -!- FUNCTION: Represses the expression of most of the genes involved in
CC oxidative stress response, such as rbr3A-rbr3B, dfx, rd, nror, fprA1
CC and fprA2, coding for reverse rubrerythrins, desulfoferrodoxin,
CC rubredoxin, NADH-rubredoxin oxidoreductase (NROR), and oxygen-reducing
CC flavoproteins, respectively. Thus, by controlling primarily oxygen and
CC reactive oxygen species (ROS) scavenging, PerR plays an important role
CC in the oxidative stress defense system in C.acetobutylicum, an obligate
CC anaerobic bacterium. Probably acts as a peroxide sensor.
CC {ECO:0000269|PubMed:18430081, ECO:0000269|PubMed:19648241}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit almost complete
CC aerotolerance and increased H(2)O(2) resistance. Deletion of perR does
CC not affect the intracellular level of iron but increases two-fold that
CC of zinc. {ECO:0000269|PubMed:18430081}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; AE001437; AAK80581.1; -; Genomic_DNA.
DR PIR; B97224; B97224.
DR RefSeq; NP_349241.1; NC_003030.1.
DR RefSeq; WP_010965922.1; NC_003030.1.
DR AlphaFoldDB; Q97FU2; -.
DR SMR; Q97FU2; -.
DR STRING; 272562.CA_C2634; -.
DR GeneID; 44999102; -.
DR KEGG; cac:CA_C2634; -.
DR PATRIC; fig|272562.8.peg.2823; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_4_2_9; -.
DR OrthoDB; 8659436at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:2000374; P:regulation of oxygen metabolic process; IMP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd07153; Fur_like; 1.
DR Gene3D; 3.30.1490.190; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002481; FUR.
DR InterPro; IPR043135; Fur_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33202:SF8; PEROXIDE-RESPONSIVE REPRESSOR PERR; 1.
DR PANTHER; PTHR33202; ZINC UPTAKE REGULATION PROTEIN; 1.
DR Pfam; PF01475; FUR; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW Detoxification; DNA-binding; Metal-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..138
FT /note="Transcriptional regulator PerR"
FT /id="PRO_0000405537"
FT REGION 1..73
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15672 MW; 34CAA30824AC357F CRC64;
MNDISTIFKE KKLKLTPQRI AVYKYLKSTH EHPSAETIYK AIQSDYPTMS LATVYKALKT
LAEVHLIQEL NVGEGNFRYD ANSSSHPHIQ CLSCGKVDDI MGITFDNLNK DVSSHTDYDV
ISNKLYFYGI CKDCKDKA
//
