PERR_STAEQ
ID PERR_STAEQ Reviewed; 150 AA.
AC Q5HN74;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Peroxide-responsive repressor PerR;
GN Name=perR; OrderedLocusNames=SERP1398;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000029; AAW54739.1; -; Genomic_DNA.
DR RefSeq; WP_001830391.1; NC_002976.3.
DR AlphaFoldDB; Q5HN74; -.
DR SMR; Q5HN74; -.
DR STRING; 176279.SERP1398; -.
DR EnsemblBacteria; AAW54739; AAW54739; SERP1398.
DR GeneID; 50018354; -.
DR KEGG; ser:SERP1398; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_4_2_9; -.
DR OMA; YLYGVCT; -.
DR OrthoDB; 1630127at2; -.
DR Proteomes; UP000000531; 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; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..150
FT /note="Peroxide-responsive repressor PerR"
FT /id="PRO_0000289020"
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; 17280 MW; 780BD8F9B170F2A8 CRC64;
MSAELESIDH ELEESIASLR KAGVRITPQR QAIMRYLISS HSHPTADEIY QALSPKFPNI
SVATIYNNLR VFKDIGIVKE LTYGDSSSRF DFNTHNHYHI ICEKCGKIVD FHYPQLDEVE
QLAQHVTDFD VTHHRMEIYG VCKECKEEGN
