ID   EFEB_YERPN              Reviewed;         434 AA.
AC   Q1CHD5; C4GUF9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Deferrochelatase;
DE            EC=4.99.1.1 {ECO:0000250|UniProtKB:P31545};
DE   AltName: Full=Peroxidase EfeB;
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:P31545};
DE   Flags: Precursor;
GN   Name=efeB; OrderedLocusNames=YPN_2267; ORFNames=YP516_2548;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC       iron from heme while preserving the protoporphyrin ring intact.
CC       {ECO:0000250|UniProtKB:P31545}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC         Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P31545};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585;
CC         Evidence={ECO:0000250|UniProtKB:P31545};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC       per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Part of a ferrous iron transporter composed of
CC       EfeU, EfeO and EfeB (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the DyP-type peroxidase family. EfeB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000305; ABG18595.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000013; EEO76346.1; -; Genomic_DNA.
DR   RefSeq; WP_002211167.1; NZ_ACNQ01000013.1.
DR   AlphaFoldDB; Q1CHD5; -.
DR   SMR; Q1CHD5; -.
DR   PeroxiBase; 5876; YpDyPrx01.
DR   EnsemblBacteria; ABG18595; ABG18595; YPN_2267.
DR   GeneID; 57976725; -.
DR   KEGG; ypn:YPN_2267; -.
DR   HOGENOM; CLU_039488_0_0_6; -.
DR   OMA; QACANDP; -.
DR   Proteomes; UP000008936; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:RHEA.
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   GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR006314; Dyp_peroxidase.
DR   InterPro; IPR006313; EfeB.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF04261; Dyp_perox; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR   TIGRFAMs; TIGR01412; tat_substr_1; 1.
DR   PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Lyase; Metal-binding; Oxidoreductase; Periplasm; Peroxidase;
KW   Signal.
FT   SIGNAL          1..45
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           46..434
FT                   /note="Deferrochelatase"
FT                   /id="PRO_0000278552"
FT   BINDING         247..249
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         340
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         345..347
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         358
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
SQ   SEQUENCE   434 AA;  47801 MW;  AA93E8FB623D41B6 CRC64;
     MRDKTGPKFG PYQPDDEAVS PSRRRLILGM GMVSGALVLG GAKTAQAADC RSPDVAGTQD
     ERWQKQPFYG QHQAGVLTPQ QAAMMLVAFD VLATDKTSLI RLFKLLTERL AFLTTGGRAP
     SVNAKLPPLD SGIMGPEIYP DNLTVTVSVG NALFDERFGL QGQKPLRLQR MTRFPNDSLD
     AGLCHGDVML QICANTNETV IHALRDIIKH TPDLLSVRWK REGFISAHAA RSKGQDTPIN
     LLGFKDGTAN PKISNKPLIN NVVWVSNNAG EPAWAVGGSY QVVRIIRFKV EFWDRTPLQE
     QQTIFGRDKN SGAPLGMQHE HDEPNYAKDP EGKVIPMDAH IRLANPRTIE TQRNLMLRRG
     YSYSLGVSNS GQLDMGLLFV CYQSDLAQAF LTVQERLNGE ALEEYVKPIG GGYFFTLPGV
     ADANHYLAQS LLEA