ID   EFEB_SHIF8              Reviewed;         421 AA.
AC   Q0T616;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=SFV_1030;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF03249.1; -; Genomic_DNA.
DR   RefSeq; WP_001199452.1; NC_008258.1.
DR   AlphaFoldDB; Q0T616; -.
DR   SMR; Q0T616; -.
DR   PeroxiBase; 5873; SflDyPrx01.
DR   EnsemblBacteria; ABF03249; ABF03249; SFV_1030.
DR   GeneID; 58391623; -.
DR   KEGG; sfv:SFV_1030; -.
DR   HOGENOM; CLU_039488_0_0_6; -.
DR   OMA; QACANDP; -.
DR   BioCyc; SFLE373384:SFV_RS05690-MON; -.
DR   Proteomes; UP000000659; 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   Repeat; Signal.
FT   SIGNAL          1..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           34..421
FT                   /note="Deferrochelatase"
FT                   /id="PRO_0000278549"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..236
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         327
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         332..334
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         345
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
SQ   SEQUENCE   421 AA;  46538 MW;  F9583A178F5B57AE CRC64;
     MQYKDENGVN EPSRRRLLKG IGALAGSCPV AHAQKTQSAP GTLSPDARNE KQPFYGEHQA
     GILTPQQAAM MLVAFDVLAS DKADLERLFR LLTQRFAFLS QGGAAPETPN PRLPPLDSGI
     LGGYIAPDNL TITLSVGHSL FDERFGLAPQ MPKKLQKMTR FPNDSLDAAL CHGDVLLQIC
     ANTQDTVNHA LRDIIKHTPD LLSVRWKREG FISDHAARSK GKETPINLLG FKDGTANPDS
     QNDKLMQKVV WVTADQQEPA WTIGGSYQAV RLIQFRVEFW DRTPLKEQQT IFGRDKQTGA
     PLGMQHEHDV PDYASDPEGK VIALDSHIRL ANPRTAESES SLMLRRGYSY SLGVTNSGQL
     DMGLLFVCYQ HDLEKGFLTV QKRLNGEALE EYVKPIGGGY FFSLPGVKDA NDYLGRALLQ
     V