ID   PERR_STAA8              Reviewed;         148 AA.
AC   Q2G282;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Peroxide-responsive repressor PerR;
GN   Name=perR; OrderedLocusNames=SAOUHSC_01997;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   CHARACTERIZATION, AND AUTOREGULATION.
RX   PubMed=11349039; DOI=10.1128/iai.69.6.3744-3754.2001;
RA   Horsburgh M.J., Clements M.O., Crossley H., Ingham E., Foster S.J.;
RT   "PerR controls oxidative stress resistance and iron storage proteins and is
RT   required for virulence in Staphylococcus aureus.";
RL   Infect. Immun. 69:3744-3754(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=12028379; DOI=10.1046/j.1365-2958.2002.02944.x;
RA   Horsburgh M.J., Wharton S.J., Cox A.G., Ingham E., Peacock S., Foster S.J.;
RT   "MntR modulates expression of the perR regulon and superoxide resistance in
RT   Staphylococcus aureus through control of manganese uptake.";
RL   Mol. Microbiol. 44:1269-1286(2002).
RN   [4]
RP   INDUCTION BY HYPOCHLOROUS ACID.
RX   PubMed=16514164; DOI=10.1099/mic.0.28385-0;
RA   Maalej S., Dammak I., Dukan S.;
RT   "The impairment of superoxide dismutase coordinates the derepression of the
RT   perR regulon in the response of Staphylococcus aureus to HOCl stress.";
RL   Microbiology 152:855-861(2006).
CC   -!- FUNCTION: Manganese-dependent repressor that controls a regulon of
CC       oxidative stress resistance and iron-storage proteins. Regulates
CC       expression of genes encoding antioxidant proteins, such as katA, ahpCF,
CC       bcp and trxB. Also regulates expression of the iron-storage protein
CC       ftn, the ferritin-like protein mrgA, the ferric uptake regulator fur,
CC       the manganese transporter operon mntABC, and its own expression. May
CC       act as a hydrogen peroxide and organic hydroperoxide sensor. Required
CC       for full virulence in a murine skin abscess model of infection.
CC       {ECO:0000269|PubMed:12028379}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Autoregulated. Induced by low levels of hypochlorous acid
CC       via superoxide dismutase inactivation. {ECO:0000269|PubMed:16514164}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31053.1; -; Genomic_DNA.
DR   RefSeq; WP_000110011.1; NZ_LS483365.1.
DR   RefSeq; YP_500494.1; NC_007795.1.
DR   AlphaFoldDB; Q2G282; -.
DR   SMR; Q2G282; -.
DR   STRING; 1280.SAXN108_1890; -.
DR   EnsemblBacteria; ABD31053; ABD31053; SAOUHSC_01997.
DR   GeneID; 3921877; -.
DR   KEGG; sao:SAOUHSC_01997; -.
DR   PATRIC; fig|93061.5.peg.1814; -.
DR   eggNOG; COG0735; Bacteria.
DR   HOGENOM; CLU_096072_4_2_9; -.
DR   OMA; YLYGVCT; -.
DR   PHI-base; PHI:4991; -.
DR   PRO; PR:Q2G282; -.
DR   Proteomes; UP000008816; Chromosome.
DR   CollecTF; EXPREG_00000d90; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR   CDD; cd07153; Fur_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.1490.190; -; 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; PTHR33202; 1.
DR   Pfam; PF01475; FUR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Manganese; Metal-binding; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..148
FT                   /note="Peroxide-responsive repressor PerR"
FT                   /id="PRO_0000289017"
FT   REGION          1..84
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  17183 MW;  F46AE99B9F367E75 CRC64;
     MSVEIESIEH ELEESIASLR QAGVRITPQR QAILRYLISS HTHPTADEIY QALSPDFPNI
     SVATIYNNLR VFKDIGIVKE LTYGDSSSRF DFNTHNHYHI ICEQCGKIVD FQYPQLNEIE
     RLAQHMTDFD VTHHRMEIYG VCKECQDK