ID   PERR_STAHJ              Reviewed;         150 AA.
AC   Q4L7G4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Peroxide-responsive repressor PerR;
GN   Name=perR; OrderedLocusNames=SH1102;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Manganese-dependent repressor that controls a regulon of
CC       oxidative stress resistance and iron-storage proteins. May act as a
CC       hydrogen peroxide and organic hydroperoxide sensor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR   EMBL; AP006716; BAE04411.1; -; Genomic_DNA.
DR   RefSeq; WP_011275403.1; NC_007168.1.
DR   AlphaFoldDB; Q4L7G4; -.
DR   SMR; Q4L7G4; -.
DR   STRING; 279808.SH1102; -.
DR   EnsemblBacteria; BAE04411; BAE04411; SH1102.
DR   KEGG; sha:SH1102; -.
DR   eggNOG; COG0735; Bacteria.
DR   HOGENOM; CLU_096072_4_2_9; -.
DR   OMA; YLYGVCT; -.
DR   OrthoDB; 1630127at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Manganese; Metal-binding; Repressor; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..150
FT                   /note="Peroxide-responsive repressor PerR"
FT                   /id="PRO_0000289021"
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   150 AA;  17301 MW;  64CF549F3B0136C5 CRC64;
     MSAELESIDH ELEESIAALR RAGVRITPQR QAIIRYLIAS HSHPTADEIY QALSPDFPNI
     SVATIYNNLR VFKSIGIVKE LTYGDASSRF DFNTHNHYHV ICEKCGKIVD FHYPQLDEVE
     QLAQHITEFD VTHHRMEIYG ICKECKDKEE