ID   EFEB_YERPS              Reviewed;         434 AA.
AC   Q66BP4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=YPTB1727;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH20966.1; -; Genomic_DNA.
DR   RefSeq; WP_011192194.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66BP4; -.
DR   SMR; Q66BP4; -.
DR   PeroxiBase; 5877; YpsDyPrx01_IP32953.
DR   EnsemblBacteria; CAH20966; CAH20966; YPTB1727.
DR   GeneID; 66841838; -.
DR   KEGG; ypo:BZ17_773; -.
DR   KEGG; yps:YPTB1727; -.
DR   PATRIC; fig|273123.14.peg.818; -.
DR   OMA; QACANDP; -.
DR   Proteomes; UP000001011; 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_0000278553"
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;  47815 MW;  5F0C4314573C0442 CRC64;
     MRDKTGPKFG PYQPDDEAVS PSRRRLILGM GMVSGALVLG GAKTAQAADC RSPDVAGTQD
     ERWQKQPFYG QHQAGVLTPQ QAAMMLVAFD VLATDKTSLI RLFKLLTERL AFLTTGGRAP
     SVNAKLPPLD SGIMGPEIYP DNLTVTVSVG NALFDERFGL QGQKPLRLQR MTRFPNDSLD
     AGLCHGDVML QICANTNETV IHALRDIIKH TPDLLSVRWK REGFISAHAA RSKGQETPIN
     LLGFKDGTAN PKISNKPLIN NVVWVSNNAG EPAWAVGGSY QVVRIIRFKV EFWDRTPLQE
     QQTIFGRDKN SGAPLGMQHE HDEPNYAKDP EGKVIPMDAH IRLANPRTIE TQRNLMLRRG
     YSYSLGVSNS GQLDMGLLFV CYQSDLAQAF LTVQERLNGE ALEEYVKPIG GGYFFTLPGV
     ADANHYLAQS LLEA