EFEB_YERPE
ID EFEB_YERPE Reviewed; 434 AA.
AC Q7CI09; Q74V02;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=YPO1856, y2450, YP_1537;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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}.
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DR EMBL; AL590842; CAL20496.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86007.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61772.1; -; Genomic_DNA.
DR PIR; AE0226; AE0226.
DR RefSeq; WP_002211167.1; NZ_WUCM01000005.1.
DR RefSeq; YP_002346850.1; NC_003143.1.
DR AlphaFoldDB; Q7CI09; -.
DR SMR; Q7CI09; -.
DR STRING; 214092.YPO1856; -.
DR PeroxiBase; 5876; YpDyPrx01.
DR PaxDb; Q7CI09; -.
DR EnsemblBacteria; AAM86007; AAM86007; y2450.
DR EnsemblBacteria; AAS61772; AAS61772; YP_1537.
DR GeneID; 57976725; -.
DR KEGG; ype:YPO1856; -.
DR KEGG; ypk:y2450; -.
DR KEGG; ypm:YP_1537; -.
DR PATRIC; fig|1028802.3.peg.27; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_039488_0_0_6; -.
DR OMA; QACANDP; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
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; 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_0000278551"
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; 47801 MW; AA93E8FB623D41B6 CRC64;
MRDKTGPKFG PYQPDDEAVS PSRRRLILGM GMVSGALVLG GAKTAQAADC RSPDVAGTQD
ERWQKQPFYG QHQAGVLTPQ QAAMMLVAFD VLATDKTSLI RLFKLLTERL AFLTTGGRAP
SVNAKLPPLD SGIMGPEIYP DNLTVTVSVG NALFDERFGL QGQKPLRLQR MTRFPNDSLD
AGLCHGDVML QICANTNETV IHALRDIIKH TPDLLSVRWK REGFISAHAA RSKGQDTPIN
LLGFKDGTAN PKISNKPLIN NVVWVSNNAG EPAWAVGGSY QVVRIIRFKV EFWDRTPLQE
QQTIFGRDKN SGAPLGMQHE HDEPNYAKDP EGKVIPMDAH IRLANPRTIE TQRNLMLRRG
YSYSLGVSNS GQLDMGLLFV CYQSDLAQAF LTVQERLNGE ALEEYVKPIG GGYFFTLPGV
ADANHYLAQS LLEA
