UniProtKB - P0ABD3 (BFR_ECOLI)
Protein
Bacterioferritin
Gene
bfr
Organism
Escherichia coli (strain K12)
Status
Functioni
Iron-storage protein, whose ferroxidase center binds Fe2+ ions, oxidizes them by dioxygen to Fe3+, and participates in the subsequent Fe3+ oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.2 Publications
Miscellaneous
The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe2+ binding and oxidation at the ferroxidase center.
Catalytic activityi
- EC:1.16.3.13 Publications
Cofactori
Protein has several cofactor binding sites:- heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.1 Publication
- Fe cation1 PublicationNote: Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.1 Publication
Activity regulationi
Iron oxidation is inhibited by Zn2+, which binds at the ferroxidase center with a higher affinity that Fe2+. The occupation of the ferroxidase center by Zn2+ also severely restricts the ability of BFR to form an iron core.3 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 18 | Iron 1PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 46 | Iron 3PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 50 | Iron 3PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 51 | Iron 1PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 51 | Iron 2PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 52 | Iron (heme axial ligand); shared with dimeric partnerPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 54 | Iron 1PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 94 | Iron 2PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 127 | Iron 1PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 127 | Iron 2PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 130 | Iron 2PROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- ferric iron binding Source: InterPro
- ferroxidase activity Source: EcoCyc
- heme binding Source: EcoCyc
- identical protein binding Source: EcoCyc
- iron ion binding Source: EcoCyc
- oxidoreductase activity Source: EcoliWiki
GO - Biological processi
- intracellular sequestering of iron ion Source: EcoCyc
- iron ion transport Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Iron storage |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10113-MONOMER MetaCyc:EG10113-MONOMER |
BRENDAi | 1.16.3.1, 2026 |
Names & Taxonomyi
Protein namesi | Recommended name: Bacterioferritin (EC:1.16.3.1)Short name: BFR Alternative name(s): Cytochrome b-1 Cytochrome b-557 |
Gene namesi | Name:bfr Ordered Locus Names:b3336, JW3298 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 18 | E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication | 1 | |
Mutagenesisi | 31 | M → H or L: No loss of heme binding. 1 Publication | 1 | |
Mutagenesisi | 46 | H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication | 1 | |
Mutagenesisi | 50 | D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication | 1 | |
Mutagenesisi | 52 | M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication | 1 | |
Mutagenesisi | 86 | M → L: No loss of heme binding. 1 Publication | 1 | |
Mutagenesisi | 127 | E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication | 1 | |
Mutagenesisi | 130 | H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000192592 | 1 – 158 | BacterioferritinAdd BLAST | 158 |
Proteomic databases
jPOSTi | P0ABD3 |
PaxDbi | P0ABD3 |
PRIDEi | P0ABD3 |
Interactioni
Subunit structurei
Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core.
7 PublicationsBinary interactionsi
P0ABD3
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-907496,EBI-907496 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4262466, 23 interactors |
DIPi | DIP-36167N |
IntActi | P0ABD3, 3 interactors |
STRINGi | 511145.b3336 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ABD3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ABD3 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 145 | Ferritin-like diironPROSITE-ProRule annotationAdd BLAST | 145 |
Sequence similaritiesi
Belongs to the bacterioferritin family.Curated
Phylogenomic databases
eggNOGi | COG2193, Bacteria |
HOGENOMi | CLU_104506_2_0_6 |
InParanoidi | P0ABD3 |
PhylomeDBi | P0ABD3 |
Family and domain databases
CDDi | cd00907, Bacterioferritin, 1 hit |
Gene3Di | 1.20.1260.10, 1 hit |
InterProi | View protein in InterPro IPR002024, Bacterioferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR008331, Ferritin_DPS_dom |
Pfami | View protein in Pfam PF00210, Ferritin, 1 hit |
PIRSFi | PIRSF002560, Bacterioferritin, 1 hit |
PRINTSi | PR00601, BACFERRITIN |
SUPFAMi | SSF47240, SSF47240, 1 hit |
TIGRFAMsi | TIGR00754, bfr, 1 hit |
PROSITEi | View protein in PROSITE PS00549, BACTERIOFERRITIN, 1 hit PS50905, FERRITIN_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ABD3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID
60 70 80 90 100
EMKHADRYIE RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN
110 120 130 140 150
LREAIGYADS VHDYVSRDMM IEILRDEEGH IDWLETELDL IQKMGLQNYL
QAQIREEG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 53 | K → M AA sequence (PubMed:2644932).Curated | 1 |
Mass spectrometryi
Molecular mass is 18496±2 Da. Determined by ESI. 1 Publication
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 5 – 7 | TKV → VKI in strain: ECOR 30. | 3 | |
Natural varianti | 38 | K → M in strain: ECOR 30. | 1 | |
Natural varianti | 57 | R → K in strain: ECOR 30. | 1 | |
Natural varianti | 68 | L → I in strain: ECOR 30. | 1 | |
Natural varianti | 78 | N → G in strain: ECOR 30. | 1 | |
Natural varianti | 88 | R → Q in strain: ECOR 30. | 1 | |
Natural varianti | 92 | A → R in strain: ECOR 30. | 1 | |
Natural varianti | 96 | D → E in strain: ECOR 30. | 1 | |
Natural varianti | 100 | N → D in strain: ECOR 30. | 1 | |
Natural varianti | 106 | G → A in strain: ECOR 30. | 1 | |
Natural varianti | 125 | R → A in strain: ECOR 30. | 1 | |
Natural varianti | 142 – 144 | QKM → GKI in strain: ECOR 30. | 3 | |
Natural varianti | 152 – 158 | AQIREEG → SQIKVKD in strain: ECOR 30. | 7 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27176 mRNA Translation: AAC13987.1 AF058450 Genomic DNA Translation: AAC14288.1 U18997 Genomic DNA Translation: AAA58133.1 U00096 Genomic DNA Translation: AAC76361.1 AP009048 Genomic DNA Translation: BAE77955.1 L28106 Genomic DNA Translation: AAC36929.1 |
PIRi | JV0032, FREC |
RefSeqi | NP_417795.1, NC_000913.3 WP_000675504.1, NZ_STEB01000038.1 |
Genome annotation databases
EnsemblBacteriai | AAC76361; AAC76361; b3336 BAE77955; BAE77955; BAE77955 |
GeneIDi | 58459569 947839 |
KEGGi | ecj:JW3298 eco:b3336 |
PATRICi | fig|1411691.4.peg.3395 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27176 mRNA Translation: AAC13987.1 AF058450 Genomic DNA Translation: AAC14288.1 U18997 Genomic DNA Translation: AAA58133.1 U00096 Genomic DNA Translation: AAC76361.1 AP009048 Genomic DNA Translation: BAE77955.1 L28106 Genomic DNA Translation: AAC36929.1 |
PIRi | JV0032, FREC |
RefSeqi | NP_417795.1, NC_000913.3 WP_000675504.1, NZ_STEB01000038.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BCF | X-ray | 2.90 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
1BFR | X-ray | 2.94 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 1-158 | [»] | |
2HTN | X-ray | 2.50 | A/B/C/D/E/F/G/H | 1-158 | [»] | |
2VXI | X-ray | 1.91 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
2Y3Q | X-ray | 1.55 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1J | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1L | X-ray | 2.50 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1M | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1N | X-ray | 2.80 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1O | X-ray | 2.95 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1P | X-ray | 2.40 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E1Q | X-ray | 2.60 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
3E2C | X-ray | 1.80 | A/B | 1-158 | [»] | |
3GHQ | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
4CVP | X-ray | 2.11 | A | 1-158 | [»] | |
4CVR | X-ray | 1.10 | A | 1-158 | [»] | |
4CVS | X-ray | 1.39 | A | 1-158 | [»] | |
4CVT | X-ray | 1.79 | A | 1-158 | [»] | |
4U3G | X-ray | 2.00 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
4XKS | X-ray | 1.57 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
4XKT | X-ray | 1.82 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
4XKU | X-ray | 1.78 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
5XGO | X-ray | 1.99 | A/B/C/D/E/F/G/H/I/J/K/L | 138-158 | [»] | |
6P8K | X-ray | 1.70 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
6P8L | X-ray | 2.10 | A/B/C/D/E/F/G/H/I/J/K/L | 1-158 | [»] | |
SMRi | P0ABD3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262466, 23 interactors |
DIPi | DIP-36167N |
IntActi | P0ABD3, 3 interactors |
STRINGi | 511145.b3336 |
Proteomic databases
jPOSTi | P0ABD3 |
PaxDbi | P0ABD3 |
PRIDEi | P0ABD3 |
Genome annotation databases
EnsemblBacteriai | AAC76361; AAC76361; b3336 BAE77955; BAE77955; BAE77955 |
GeneIDi | 58459569 947839 |
KEGGi | ecj:JW3298 eco:b3336 |
PATRICi | fig|1411691.4.peg.3395 |
Organism-specific databases
EchoBASEi | EB0111 |
Phylogenomic databases
eggNOGi | COG2193, Bacteria |
HOGENOMi | CLU_104506_2_0_6 |
InParanoidi | P0ABD3 |
PhylomeDBi | P0ABD3 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10113-MONOMER MetaCyc:EG10113-MONOMER |
BRENDAi | 1.16.3.1, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0ABD3 |
PROi | PR:P0ABD3 |
Family and domain databases
CDDi | cd00907, Bacterioferritin, 1 hit |
Gene3Di | 1.20.1260.10, 1 hit |
InterProi | View protein in InterPro IPR002024, Bacterioferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR008331, Ferritin_DPS_dom |
Pfami | View protein in Pfam PF00210, Ferritin, 1 hit |
PIRSFi | PIRSF002560, Bacterioferritin, 1 hit |
PRINTSi | PR00601, BACFERRITIN |
SUPFAMi | SSF47240, SSF47240, 1 hit |
TIGRFAMsi | TIGR00754, bfr, 1 hit |
PROSITEi | View protein in PROSITE PS00549, BACTERIOFERRITIN, 1 hit PS50905, FERRITIN_LIKE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BFR_ECOLI | |
Accessioni | P0ABD3Primary (citable) accession number: P0ABD3 Secondary accession number(s): O68931, P11056, Q2M701 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 25, 2005 |
Last sequence update: | October 25, 2005 | |
Last modified: | April 7, 2021 | |
This is version 122 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families