ID BFR_PSEAE Reviewed; 154 AA. AC Q9HWF9; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Bacterioferritin; DE Short=BFR; DE EC=1.16.3.1; GN Name=bfr; Synonyms=bfrA; OrderedLocusNames=PA4235; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) CC ions, oxidizes them by dioxygen to Fe(3+), and participates in the CC subsequent Fe(3+) oxide mineral core formation within the central CC cavity of the protein complex. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000305}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron- CC binding site within each subunit is known as the ferroxidase center. CC {ECO:0000250}; CC -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that are CC packed together to form an approximately spherical molecule with a CC central cavity, in which large amounts of iron can be deposited. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG07623.1; -; Genomic_DNA. DR PIR; A83113; A83113. DR RefSeq; NP_252925.1; NC_002516.2. DR RefSeq; WP_003093668.1; NZ_QZGE01000028.1. DR PDB; 3R2H; X-ray; 1.70 A; A=1-154. DR PDB; 3R2K; X-ray; 1.55 A; A=1-154. DR PDB; 3R2L; X-ray; 1.85 A; A=1-154. DR PDB; 3R2M; X-ray; 1.80 A; A=1-154. DR PDB; 3R2O; X-ray; 1.95 A; A=1-154. DR PDB; 3R2R; X-ray; 1.65 A; A=1-154. DR PDB; 3R2S; X-ray; 2.10 A; A=1-154. DR PDBsum; 3R2H; -. DR PDBsum; 3R2K; -. DR PDBsum; 3R2L; -. DR PDBsum; 3R2M; -. DR PDBsum; 3R2O; -. DR PDBsum; 3R2R; -. DR PDBsum; 3R2S; -. DR AlphaFoldDB; Q9HWF9; -. DR SMR; Q9HWF9; -. DR STRING; 208964.PA4235; -. DR PaxDb; 208964-PA4235; -. DR GeneID; 77219226; -. DR GeneID; 881830; -. DR KEGG; pae:PA4235; -. DR PATRIC; fig|208964.12.peg.4436; -. DR PseudoCAP; PA4235; -. DR HOGENOM; CLU_104506_2_0_6; -. DR InParanoid; Q9HWF9; -. DR OrthoDB; 9800505at2; -. DR PhylomeDB; Q9HWF9; -. DR BioCyc; PAER208964:G1FZ6-4308-MONOMER; -. DR EvolutionaryTrace; Q9HWF9; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:PseudoCAP. DR GO; GO:0006826; P:iron ion transport; IDA:PseudoCAP. DR CDD; cd00907; Bacterioferritin; 1. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR012347; Ferritin-like. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR008331; Ferritin_DPS_dom. DR NCBIfam; TIGR00754; bfr; 1. DR PANTHER; PTHR30295; BACTERIOFERRITIN; 1. DR PANTHER; PTHR30295:SF9; BACTERIOFERRITIN; 1. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF002560; Bacterioferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Iron storage; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..154 FT /note="Bacterioferritin" FT /id="PRO_0000287751" FT DOMAIN 1..145 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 18 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 48 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_note="ligand shared between dimeric partners" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 93 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT HELIX 5..34 FT /evidence="ECO:0007829|PDB:3R2K" FT HELIX 38..64 FT /evidence="ECO:0007829|PDB:3R2K" FT HELIX 82..109 FT /evidence="ECO:0007829|PDB:3R2K" FT HELIX 113..128 FT /evidence="ECO:0007829|PDB:3R2K" FT HELIX 130..144 FT /evidence="ECO:0007829|PDB:3R2K" FT HELIX 146..152 FT /evidence="ECO:0007829|PDB:3R2K" SQ SEQUENCE 154 AA; 17940 MW; DFD36D0DB9518343 CRC64; MQGHPEVIDY LNTLLTGELA ARDQYFIHSR MYEDWGFSKL YERLNHEMEE ETQHADALLR RILLLEGTPR MRPDDIHPGT TVPEMLEADL KLERHVRAAL AKGIALCEQH KDFVSRDILK AQLADTEEDH AYWLEQQLGL IARMGLENYL QSQI //