PERR_BACSU
ID PERR_BACSU Reviewed; 145 AA.
AC P71086;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Peroxide operon regulator;
GN Name=perR; Synonyms=ygaG; OrderedLocusNames=BSU08730;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202460; DOI=10.1099/00221287-143-6-1855;
RA Cummings N.J., Connerton I.F.;
RT "The Bacillus subtilis 168 chromosome from sspE to katA.";
RL Microbiology 143:1855-1859(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9701813; DOI=10.1046/j.1365-2958.1998.00921.x;
RA Bsat N., Herbig A., Casillas-Martinez L., Setlow P., Helmann J.D.;
RT "Bacillus subtilis contains multiple Fur homologues: identification of the
RT iron uptake (Fur) and peroxide regulon (PerR) repressors.";
RL Mol. Microbiol. 29:189-198(1998).
RN [4]
RP MUTAGENESIS OF CYS-136 AND CYS-139.
RX PubMed=12100544; DOI=10.1046/j.1365-2958.2002.03015.x;
RA Mongkolsuk S., Helmann J.D.;
RT "Regulation of inducible peroxide stress responses.";
RL Mol. Microbiol. 45:9-15(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT, AND ZINC-BINDING SITES.
RX PubMed=16925555; DOI=10.1111/j.1365-2958.2006.05313.x;
RA Traore D.A., El Ghazouani A., Ilango S., Dupuy J., Jacquamet L.,
RA Ferrer J.-L., Caux-Thang C., Duarte V., Latour J.-M.;
RT "Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis.";
RL Mol. Microbiol. 61:1211-1219(2006).
CC -!- FUNCTION: Hydrogen and organic peroxide sensor. Represses the
CC expression of a regulon of peroxide-inducible genes such as katA, ahpC,
CC ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and
CC mrgA.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16925555}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Possibly oxidized on a cysteine residue; the Cys-SOH formed in
CC response to oxidative signaling may rapidly react with a Cys-SH to form
CC a disulfide bond, leading to the loss of metal ion and inactivation of
CC repressor function. Oxidized PerR can be further reduced by thiol
CC reductants and repressor activity restored.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; Z82044; CAB04800.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12701.1; -; Genomic_DNA.
DR PIR; B69816; B69816.
DR RefSeq; NP_388753.1; NC_000964.3.
DR RefSeq; WP_003223285.1; NZ_JNCM01000032.1.
DR PDB; 2FE3; X-ray; 1.75 A; A/B=1-145.
DR PDB; 2RGV; X-ray; 2.05 A; A/B=1-145.
DR PDB; 3F8N; X-ray; 3.15 A; A/B=1-145.
DR PDBsum; 2FE3; -.
DR PDBsum; 2RGV; -.
DR PDBsum; 3F8N; -.
DR AlphaFoldDB; P71086; -.
DR SMR; P71086; -.
DR STRING; 224308.BSU08730; -.
DR PaxDb; P71086; -.
DR PRIDE; P71086; -.
DR EnsemblBacteria; CAB12701; CAB12701; BSU_08730.
DR GeneID; 64302726; -.
DR GeneID; 939227; -.
DR KEGG; bsu:BSU08730; -.
DR PATRIC; fig|224308.179.peg.941; -.
DR eggNOG; COG0735; Bacteria.
DR InParanoid; P71086; -.
DR OMA; YLYGVCT; -.
DR PhylomeDB; P71086; -.
DR BioCyc; BSUB:BSU08730-MON; -.
DR EvolutionaryTrace; P71086; -.
DR PRO; PR:P71086; -.
DR Proteomes; UP000001570; Chromosome.
DR CollecTF; EXPREG_00000bc0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
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 3D-structure; Cytoplasm; Disulfide bond; DNA-binding; Manganese;
KW Metal-binding; Oxidation; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..145
FT /note="Peroxide operon regulator"
FT /id="PRO_0000095590"
FT REGION 1..78
FT /note="DNA-binding"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 136
FT /note="C->S: No repressor activity."
FT /evidence="ECO:0000269|PubMed:12100544"
FT MUTAGEN 139
FT /note="C->D: Full repressor activity, but no modulation by
FT peroxide."
FT /evidence="ECO:0000269|PubMed:12100544"
FT MUTAGEN 139
FT /note="C->H: Full repressor activity, but no modulation by
FT peroxide."
FT /evidence="ECO:0000269|PubMed:12100544"
FT MUTAGEN 139
FT /note="C->S: No repressor activity."
FT /evidence="ECO:0000269|PubMed:12100544"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:2FE3"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2FE3"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3F8N"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2FE3"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2FE3"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2FE3"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2FE3"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:2FE3"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:2FE3"
SQ SEQUENCE 145 AA; 16424 MW; 8E864B148BD3BE97 CRC64;
MAAHELKEAL ETLKETGVRI TPQRHAILEY LVNSMAHPTA DDIYKALEGK FPNMSVATVY
NNLRVFRESG LVKELTYGDA SSRFDFVTSD HYHAICENCG KIVDFHYPGL DEVEQLAAHV
TGFKVSHHRL EIYGVCQECS KKENH
