ID   EFEB_ECOK1              Reviewed;         423 AA.
AC   A1A9S3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Deferrochelatase;
DE            EC=4.98.1.1 {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=Ecok1_09190;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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=4.98.1.1;
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; CP000468; ABJ00413.1; -; Genomic_DNA.
DR   RefSeq; WP_001199136.1; NZ_CADILS010000016.1.
DR   AlphaFoldDB; A1A9S3; -.
DR   SMR; A1A9S3; -.
DR   PeroxiBase; 5878; EcoDyPrx01_APECO1.
DR   KEGG; ecv:APECO1_110; -.
DR   HOGENOM; CLU_039488_0_0_6; -.
DR   Proteomes; UP000008216; 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; IPR048328; Dyp_perox_C.
DR   InterPro; IPR048327; Dyp_perox_N.
DR   InterPro; IPR006314; Dyp_peroxidase.
DR   InterPro; IPR006313; EfeB/EfeN.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR01413; Dyp_perox_fam; 1.
DR   NCBIfam; TIGR01412; tat_substr_1; 1.
DR   PANTHER; PTHR30521:SF4; DEFERROCHELATASE; 1.
DR   PANTHER; PTHR30521; DEFERROCHELATASE/PEROXIDASE; 1.
DR   Pfam; PF20628; Dyp_perox_C; 1.
DR   Pfam; PF04261; Dyp_perox_N; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 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   Reference proteome; 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_0000278545"
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;  46654 MW;  9EB660519206CD2E 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
     DSQNDKLMQK VVWVTADQQE PAWTIGGSYQ AVRLIQFRVE FWDRTPLKEQ QTIFGRDKQT
     GAPLGMLHEH DVPDYASDPE GKVIALDSHI RLANPRTAES ESSLMLRRGY SYSLGVTNSG
     QLDMGLLFVC YQHDLEKGFL TVQKRLNGEA LEEYVKPIGG GYFFALSGVK DANDYLGSAL
     LRV
//