ID   DYP_RHOE4               Reviewed;         341 AA.
AC   C0ZVK5;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Dye-decolorizing peroxidase {ECO:0000303|PubMed:24981030};
DE            Short=DypB {ECO:0000303|PubMed:24981030};
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:P76536};
GN   OrderedLocusNames=RER_59910;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RC   STRAIN=N771;
RX   PubMed=24981030; DOI=10.1002/bit.25322;
RA   Tamura A., Fukutani Y., Takami T., Fujii M., Nakaguchi Y., Murakami Y.,
RA   Noguchi K., Yohda M., Odaka M.;
RT   "Packaging guest proteins into the encapsulin nanocompartment from
RT   Rhodococcus erythropolis N771.";
RL   Biotechnol. Bioeng. 112:13-20(2015).
CC   -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment
CC       (PubMed:24981030). Has both general peroxidase activity and dye-
CC       decolorizing activity. Can catalyze the oxidation of both
CC       protoporphyrinogen IX and coproporphyrinogen III to their corresponding
CC       porphyrins. Also efficiently decolorizes the dyes alizarin red and
CC       Cibacron blue F3GA (By similarity). This cargo-loaded encapsulin
CC       nanocompartment is probably involved in protection against oxidative
CC       damage (By similarity). {ECO:0000250|UniProtKB:I6WZG6,
CC       ECO:0000250|UniProtKB:P76536, ECO:0000269|PubMed:24981030}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P76536};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:A0A3T0E4B9}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000269|PubMed:24981030}.
CC   -!- DOMAIN: The C-terminal 38 residues (targeting peptide, TP) are
CC       sufficient to target this foreign proteins to the nanocompartment in
CC       vivo. {ECO:0000269|PubMed:24981030}.
CC   -!- BIOTECHNOLOGY: The 38 C-terminal residues can be used to target foreign
CC       proteins to the nanocompartment. {ECO:0000269|PubMed:24981030}.
CC   -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR   EMBL; AP008957; BAH36699.1; -; Genomic_DNA.
DR   STRING; 234621.RER_59910; -.
DR   EnsemblBacteria; BAH36699; BAH36699; RER_59910.
DR   KEGG; rer:RER_59910; -.
DR   eggNOG; COG2837; Bacteria.
DR   HOGENOM; CLU_044178_1_0_11; -.
DR   OMA; CAEPNLH; -.
DR   Proteomes; UP000002204; 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..341
FT                   /note="Dye-decolorizing peroxidase"
FT                   /id="PRO_0000455328"
FT   REGION          304..341
FT                   /note="Targeting peptide"
FT                   /evidence="ECO:0000269|PubMed:24981030"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q47KB1"
FT   BINDING         221
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:Q8XBI9"
SQ   SEQUENCE   341 AA;  36959 MW;  2485402CEA58CDFC CRC64;
     MALPAIPQPL LTPLTEAAIF LVFTIDEGGE QAVHDVLADI SGLQRSIGFR VPAGGLAAVV
     GIGSDAWDRL FEGPRPAELH PFVELTGDKH HAPRTPGDLL FHIRARQMDL CFEFATVVTN
     RLAGAASVID EVHGFKYFEQ RDLMGFVDGT ENPSGQAAYV AVTVGDEDPD FAGSSYVIVQ
     KYLHDMSEWN SLPVEEQENV IGRSKLEDLE MDDDTKPANS HTALTVIEDE SGEQIQILRD
     NMPFGHVGSA EMGTYFIGYS ASPTVTEQML TNMFIGNPVG NYDRILDFST AVTGINFFVP
     TADFLDDPPD APTRLVPEAT FTAPISDGSL GIGSLKRSAQ Q