ID   EFEB_ECOL5              Reviewed;         423 AA.
AC   Q0TJ48;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=ECP_1018;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG69031.1; -; Genomic_DNA.
DR   RefSeq; WP_001199132.1; NC_008253.1.
DR   AlphaFoldDB; Q0TJ48; -.
DR   SMR; Q0TJ48; -.
DR   STRING; 362663.ECP_1018; -.
DR   PeroxiBase; 5868; EcoDyPrx01_536.
DR   EnsemblBacteria; ABG69031; ABG69031; ECP_1018.
DR   KEGG; ecp:ECP_1018; -.
DR   HOGENOM; CLU_039488_0_0_6; -.
DR   OMA; QACANDP; -.
DR   Proteomes; UP000009182; 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..35
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           36..423
FT                   /note="Deferrochelatase"
FT                   /id="PRO_0000278546"
FT   BINDING         236..238
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         329
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         334..336
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
FT   BINDING         347
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P31545"
SQ   SEQUENCE   423 AA;  46620 MW;  6CDEF38C2703CEF3 CRC64;
     MQYEDENGVN EPSRRRLLKG IGALALAGSC PVAHAQKTQS APGTLSPDAR NEKQPFYGEH
     QAGILTPQQA AMMLVAFDVL ASDKADLERL FRLLTQRFAF LTQGGAAPET PNPRLPPLDS
     GILGGYIAPD NLTITLSVGH SLFDERFGLA PQMPKKLQKM TRFPNDSLDA ALCHGDVLLQ
     ICANTQDTVI HALRDIIKHT PDLLSVRWKR EGFISDHAAR SKGKETPINL LGFKDGTANP
     DSQNAKLMQK VVWVTADQQE PAWTIGGSYQ AVRLIQFRVE FWDRTPLKEQ QTIFGRDKQT
     GAPLGMLHEH DVPDYASDPE GKVIALDSHI RLANPRTAES ESSLMLRRGY SYSLGVTNSG
     QLDMGLLFVC YQHDLEKGFL TVQKRLNGEA LEEYVKPIGG GYFFALPGVK DANDYLGSAL
     LRV