EFEN_BACSU
ID EFEN_BACSU Reviewed; 416 AA.
AC P39597;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Deferrochelatase;
DE EC=4.99.1.1 {ECO:0000250|UniProtKB:P31545};
DE AltName: Full=Peroxidase EfeN;
DE EC=1.11.1.- {ECO:0000250|UniProtKB:P31545};
DE Flags: Precursor;
GN Name=efeN; Synonyms=ywbN; OrderedLocusNames=BSU38260; ORFNames=ipa-29d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP EXPORT VIA THE TAT-SYSTEM.
RX PubMed=15554971; DOI=10.1111/j.1365-2958.2004.04341.x;
RA Jongbloed J.D.H., Grieger U., Antelmann H., Hecker M., Nijland R., Bron S.,
RA van Dijl J.M.;
RT "Two minimal Tat translocases in Bacillus.";
RL Mol. Microbiol. 54:1319-1325(2004).
RN [4]
RP FUNCTION IN IRON UPTAKE.
RC STRAIN=168 / CU1065;
RX PubMed=16672620; DOI=10.1128/jb.188.10.3664-3673.2006;
RA Ollinger J., Song K.-B., Antelmann H., Hecker M., Helmann J.D.;
RT "Role of the Fur regulon in iron transport in Bacillus subtilis.";
RL J. Bacteriol. 188:3664-3673(2006).
CC -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC iron from heme while preserving the protoporphyrin ring intact (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16672620}.
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 {ECO:0000250};
CC -!- SUBUNIT: Part of a ferrous iron transporter composed of EfeU, EfeM and
CC EfeN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR EMBL; X73124; CAA51585.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15852.1; -; Genomic_DNA.
DR PIR; S39684; S39684.
DR RefSeq; NP_391705.1; NC_000964.3.
DR RefSeq; WP_003243445.1; NZ_JNCM01000034.1.
DR PDB; 6KMM; X-ray; 1.93 A; A/B/C/D/E/F=55-416.
DR PDB; 6KMN; X-ray; 2.44 A; A/B/C/D=55-416.
DR PDBsum; 6KMM; -.
DR PDBsum; 6KMN; -.
DR AlphaFoldDB; P39597; -.
DR SMR; P39597; -.
DR STRING; 224308.BSU38260; -.
DR PeroxiBase; 5874; BsDyPrx01.
DR jPOST; P39597; -.
DR PaxDb; P39597; -.
DR PRIDE; P39597; -.
DR EnsemblBacteria; CAB15852; CAB15852; BSU_38260.
DR GeneID; 937310; -.
DR KEGG; bsu:BSU38260; -.
DR PATRIC; fig|224308.179.peg.4142; -.
DR eggNOG; COG2837; Bacteria.
DR InParanoid; P39597; -.
DR OMA; QACANDP; -.
DR PhylomeDB; P39597; -.
DR BioCyc; BSUB:BSU38260-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; 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 InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF04261; Dyp_perox; 1.
DR Pfam; PF10518; TAT_signal; 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 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Lyase; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 29..416
FT /note="Deferrochelatase"
FT /id="PRO_0000013735"
FT REGION 293..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P31545"
FT BINDING 326
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 339
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P31545"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:6KMM"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6KMN"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6KMN"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:6KMM"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:6KMM"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 353..366
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:6KMM"
FT STRAND 389..399
FT /evidence="ECO:0007829|PDB:6KMM"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6KMM"
SQ SEQUENCE 416 AA; 45693 MW; AC9981A7631FACCE CRC64;
MSDEQKKPEQ IHRRDILKWG AMAGAAVAIG ASGLGGLAPL VQTAAKPSKK DEKEEEQIVP
FYGKHQAGIT TAHQTYVYFA ALDVTAKDKS DIITLFRNWT SLTQMLTSGK KMSAEQRNQY
LPPQDTGESA DLSPSNLTVT FGFGPGFFEK DGKDRFGLKS KKPKHLAALP AMPNDNLDEK
QGGGDICIQV CADDEQVAFH ALRNLLNQAV GTCEVRFVNK GFLSGGKNGE TPRNLFGFKD
GTGNQSTKDD TLMNSIVWIQ SGEPDWMTGG TYMAFRKIKM FLEVWDRSSL KDQEDTFGRR
KSSGAPFGQK KETDPVKLNQ IPSNSHVSLA KSTGKQILRR AFSYTEGLDP KTGYMDAGLL
FISFQKNPDN QFIPMLKALS AKDALNEYTQ TIGSALYACP GGCKKGEYIA QRLLES
