ID   DYP_BRELN               Reviewed;         367 AA.
AC   A0A3T0E4B9;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Dye-decolorizing peroxidase {ECO:0000303|PubMed:19172747};
DE            Short=DyP {ECO:0000303|PubMed:19172747};
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:P76536};
GN   ORFNames=CXR29_00095;
OS   Brevibacterium linens.
OC   Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; Brevibacterium.
OX   NCBI_TaxID=1703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19391;
RX   PubMed=31244798; DOI=10.3389/fmicb.2019.01270;
RA   Levesque S., de Melo A.G., Labrie S.J., Moineau S.;
RT   "Mobilome of Brevibacterium aurantiacum Sheds Light on Its Genetic
RT   Diversity and Its Adaptation to Smear-Ripened Cheeses.";
RL   Front. Microbiol. 10:1270-1270(2019).
RN   [2]
RP   PROBABLE SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC   STRAIN=M18;
RX   PubMed=19172747; DOI=10.1038/nsmb.1473;
RA   Sutter M., Boehringer D., Gutmann S., Gunther S., Prangishvili D.,
RA   Loessner M.J., Stetter K.O., Weber-Ban E., Ban N.;
RT   "Structural basis of enzyme encapsulation into a bacterial
RT   nanocompartment.";
RL   Nat. Struct. Mol. Biol. 15:939-947(2008).
CC   -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. Has
CC       both general peroxidase activity and dye-decolorizing activity. Can
CC       catalyze the oxidation of both protoporphyrinogen IX and
CC       coproporphyrinogen III to their corresponding porphyrins. Also
CC       efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA
CC       (By similarity). This cargo-loaded encapsulin nanocompartment is
CC       probably involved in protection against oxidative damage (By
CC       similarity). {ECO:0000250|UniProtKB:I6WZG6,
CC       ECO:0000250|UniProtKB:P76536}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P76536};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000305|PubMed:19172747}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000269|PubMed:19172747}.
CC   -!- DOMAIN: The C-terminus (at least 10 residues, not detailed in paper)
CC       targets the protein to the nanocompartment.
CC       {ECO:0000305|PubMed:19172747}.
CC   -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR   EMBL; CP026734; AZU02205.1; -; Genomic_DNA.
DR   EnsemblBacteria; AZU02205; AZU02205; CXR29_00095.
DR   Proteomes; UP000282883; Chromosome.
DR   GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR006314; Dyp_peroxidase.
DR   Pfam; PF04261; Dyp_perox; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR   PROSITE; PS51404; DYP_PEROXIDASE; 1.
PE   1: Evidence at protein level;
KW   Encapsulin nanocompartment; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..367
FT                   /note="Dye-decolorizing peroxidase"
FT                   /id="PRO_0000455325"
FT   REGION          311..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..365
FT                   /note="Targeting peptide"
FT                   /evidence="ECO:0000305|PubMed:19172747"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q47KB1"
FT   BINDING         225
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q47KB1"
SQ   SEQUENCE   367 AA;  39926 MW;  70AF1BF5D5446BB9 CRC64;
     MTEAFPNGKT PQHVLGPPAP AAVFLVLTVR SGAEAEAKDF LGDIAGVVRS VGFRAREDHL
     SCVTGIGAEL WDRMFDAPRP AGLHPFIEQR GDVHTAPSTP GDLLFHIRAR RMDLCFELAR
     QLVGELGDAV SVVDEVHGFR YFDERDIMGF VDGTENPEDQ EAVDSVFTPT GGDDPASSTY
     VIVQKYTHDM AAWEALSVED QEAAFGRHKL SDMEFPDEDK APNSHLILNT IEDEDGTEHK
     IVRDNMVFGS VESGEFGTYF IGYAADVSVT EQMLENMFIG NPRGTYDRIL DFSTAQTGGL
     FFVPSQDFLD DPDGELAAAE PSDAQNDDPA SASARIEETD PPNPASADDP APADDSLGIG
     SLRRRDQ