BFR_PSEAE
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 03-AUG-2022, entry version 115.
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; Proteobacteria; 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 / 1C /
RC 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}.
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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; 287.DR97_3676; -.
DR PaxDb; Q9HWF9; -.
DR PRIDE; Q9HWF9; -.
DR EnsemblBacteria; AAG07623; AAG07623; PA4235.
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 OMA; LYERIDH; -.
DR PhylomeDB; Q9HWF9; -.
DR BioCyc; PAER208964:G1FZ6-4308-MON; -.
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 Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF002560; Bacterioferritin; 1.
DR PRINTS; PR00601; BACFERRITIN.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR00754; bfr; 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
