ID   DYP_MYCPA               Reviewed;         354 AA.
AC   Q743F4;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Dye-decolorizing peroxidase {ECO:0000303|PubMed:25500374};
DE            Short=DyP {ECO:0000303|PubMed:25500374};
DE            EC=1.11.1.7 {ECO:0000250|UniProtKB:I6Y4U9};
GN   OrderedLocusNames=MAP_0631c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TYPE 1 ENCAPSULIN,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND ANTIGENICITY.
RC   STRAIN=509;
RX   PubMed=25500374; DOI=10.1016/j.vetmic.2014.11.009;
RA   Leite F.L., Reinhardt T.A., Bannantine J.P., Stabel J.R.;
RT   "Envelope protein complexes of Mycobacterium avium subsp. paratuberculosis
RT   and their antigenicity.";
RL   Vet. Microbiol. 175:275-285(2015).
CC   -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A heme-
CC       dependent peroxidase (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:I6Y4U9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC         H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC         Evidence={ECO:0000250|UniProtKB:I6Y4U9};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:I6Y4U9};
CC   -!- SUBUNIT: Found in a complex with type 1 encapsulin, strongly suggesting
CC       it is found in a type 1 encapsulin nanocompartment (PubMed:25500374).
CC       Homotetramer, presumably also in the type 1 encapsulin nanocompartment
CC       (By similarity). {ECO:0000250|UniProtKB:I6Y4U9,
CC       ECO:0000269|PubMed:25500374}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000250|UniProtKB:A0A3T0E4B9, ECO:0000305}. Cell membrane
CC       {ECO:0000305|PubMed:25500374}.
CC   -!- DOMAIN: The C-terminus (residues 312-335) targets the protein to the
CC       type 1 encapsulin nanocompartment. {ECO:0000250|UniProtKB:I6Y4U9}.
CC   -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR   EMBL; AE016958; AAS02948.1; -; Genomic_DNA.
DR   STRING; 262316.MAP_0631c; -.
DR   PeroxiBase; 5527; MavpDyPrx02.
DR   EnsemblBacteria; AAS02948; AAS02948; MAP_0631c.
DR   KEGG; mpa:MAP_0631c; -.
DR   eggNOG; COG2837; Bacteria.
DR   HOGENOM; CLU_044178_1_0_11; -.
DR   OMA; CAEPNLH; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell membrane; Encapsulin nanocompartment; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Dye-decolorizing peroxidase"
FT                   /id="PRO_0000455326"
FT   REGION          312..335
FT                   /note="Targeting peptide"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y4U9"
FT   REGION          324..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q47KB1"
FT   BINDING         238
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   354 AA;  38411 MW;  81831906637C6F90 CRC64;
     MVNIVAVRRH GVHVRVIHVP PVQPQPILAP LTPAAIFLVL TVDDGGEATV HEALQDISGL
     VRAIGFREPQ KRLSAIASIG SDVWDRLFSG PRPAELHRFV ELHGPRHTAP ATPGDLLFHI
     RAESLDVCFE LADRILKSMA GAVTVVDEVH GFRYFDNRDL LGFVDGTENP DGALAVSSTA
     IGDEDPDFAG SCYVHVQKYL HDMSAWTALS VTEQENVIGR TKLDDIELDD DVKPADAHIA
     LNVITDDDGT ELKIVRHNMP FGELGKSEYG TYFIGYSRTP RVTEQMLRNM FLGDPPGNTD
     RILDFSTAVT GGLFFSPTVD FLDDPPPLPA PGTPAAPPAR NGSLSIGSLK GTTR