EFEB_SHIFL
ID EFEB_SHIFL Reviewed; 421 AA.
AC Q83LK4; Q7C248;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SF1021, S1091;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42647.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16532.1; -; Genomic_DNA.
DR RefSeq; NP_706940.1; NC_004337.2.
DR RefSeq; WP_001199452.1; NZ_WPGW01000205.1.
DR AlphaFoldDB; Q83LK4; -.
DR SMR; Q83LK4; -.
DR STRING; 198214.SF1021; -.
DR PeroxiBase; 5873; SflDyPrx01.
DR EnsemblBacteria; AAN42647; AAN42647; SF1021.
DR EnsemblBacteria; AAP16532; AAP16532; S1091.
DR GeneID; 1026238; -.
DR GeneID; 58391623; -.
DR KEGG; sfl:SF1021; -.
DR KEGG; sfx:S1091; -.
DR PATRIC; fig|198214.7.peg.1185; -.
DR HOGENOM; CLU_039488_0_0_6; -.
DR OMA; QACANDP; -.
DR OrthoDB; 837319at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Reference proteome; 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_0000278548"
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