Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0ABD3 (BFR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacterioferritin

Short name=BFR
EC=1.16.3.1
Alternative name(s):
Cytochrome b-1
Cytochrome b-557
Gene names
Name:bfr
Ordered Locus Names:b3336, JW3298
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O. Ref.9 Ref.10 Ref.14

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.7 Ref.15

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. Ref.15

Enzyme regulation

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. Ref.9 Ref.10 Ref.14

Subunit structure

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. Ref.12

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.

Sequence similarities

Belongs to the bacterioferritin family.

Contains 1 ferritin-like diiron domain.

Mass spectrometry

Molecular mass is 18496±2 Da from positions 1 - 158. Determined by ESI. Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Bacterioferritin
PRO_0000192592

Regions

Domain1 – 145145Ferritin-like diiron

Sites

Metal binding181Iron 1
Metal binding461Iron 3
Metal binding501Iron 3
Metal binding511Iron 1
Metal binding511Iron 2
Metal binding521Iron (heme axial ligand); shared with dimeric partner
Metal binding541Iron 1
Metal binding941Iron 2
Metal binding1271Iron 1
Metal binding1271Iron 2
Metal binding1301Iron 2

Natural variations

Natural variant5 – 73TKV → VKI in strain: ECOR 30.
Natural variant381K → M in strain: ECOR 30.
Natural variant571R → K in strain: ECOR 30.
Natural variant681L → I in strain: ECOR 30.
Natural variant781N → G in strain: ECOR 30.
Natural variant881R → Q in strain: ECOR 30.
Natural variant921A → R in strain: ECOR 30.
Natural variant961D → E in strain: ECOR 30.
Natural variant1001N → D in strain: ECOR 30.
Natural variant1061G → A in strain: ECOR 30.
Natural variant1251R → A in strain: ECOR 30.
Natural variant142 – 1443QKM → GKI in strain: ECOR 30.
Natural variant152 – 1587AQIREEG → SQIKVKD in strain: ECOR 30.

Experimental info

Mutagenesis181E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. Ref.10
Mutagenesis311M → H or L: No loss of heme binding. Ref.7
Mutagenesis461H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. Ref.15
Mutagenesis501D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. Ref.15
Mutagenesis521M → H or L: Loss of heme binding. Is still capable of accumulating iron. Ref.7
Mutagenesis861M → L: No loss of heme binding. Ref.7
Mutagenesis1271E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. Ref.10
Mutagenesis1301H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. Ref.10
Sequence conflict531K → M AA sequence Ref.5

Secondary structure

........... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABD3 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: A6C86CE1CD8F865A

FASTA15818,495
        10         20         30         40         50         60 
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE 

        70         80         90        100        110        120 
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM 

       130        140        150 
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12."
Andrews S.C., Harrison P.M., Guest J.R.
J. Bacteriol. 171:3940-3947(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]Noorani S.M., Lindahl L., Zengel J.M.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ECOR 30.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia coli-K12."
Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.
Biochem. Biophys. Res. Commun. 158:489-496(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-87.
Strain: K12.
[6]"Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria."
Whitchurch C.B., Mattick J.S.
Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
Strain: K12.
[7]"Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants."
Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R., Guest J.R., Harrison P.M.
J. Biol. Chem. 270:23268-23274(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: HEME-BINDING, MASS SPECTROMETRY, MUTAGENESIS OF MET-31; MET-52 AND MET-86.
Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin."
Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.
Biochemistry 39:4915-4923(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[10]"Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center."
Baaghil S., Lewin A., Moore G.R., Le Brun N.E.
Biochemistry 42:14047-14056(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF GLU-18; GLU-127 AND HIS-130.
[11]"Structure of a unique twofold symmetric haem-binding site."
Frolow F., Kalb A.J., Yariv J.
Nat. Struct. Biol. 1:453-460(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS.
[12]"Structure of a monoclinic crystal form of cyctochrome b1 (bacterioferritin) from E. coli."
Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M., Kalb A.J., Frolow F.
Acta Crystallogr. D 54:16-24(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS, SUBUNIT.
[13]"Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form."
van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.
Acta Crystallogr. F 62:1061-1066(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND ZINC IONS.
Strain: B / BL21.
[14]"Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy."
Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.
Biochemistry 48:9031-9039(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, ENZYME REGULATION.
Strain: K12 / JM109 / ATCC 53323.
[15]"Structural basis for iron mineralization by bacterioferritin."
Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.
J. Am. Chem. Soc. 131:6808-6813(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF METAL-FREE APOPROTEIN AND IN COMPLEXES WITH ZN(2+); FE(2+); FE(3+) AND HEME, COFACTOR, INTERNAL SURFACE IRON-BINDING SITE, MUTAGENESIS OF HIS-46 AND ASP-50, MECHANISM OF IRON MINERALIZATION.
Strain: K12 / JM109 / ATCC 53323.
[16]"Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation."
Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R., Murphy M.E., Mauk A.G.
J. Biol. Chem. 284:18873-18881(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER IN COMPLEX WITH HEME AND ZINC IONS.
[17]"The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin."
Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.
J. Biol. Inorg. Chem. 14:201-207(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC IONS.
Strain: B / BL21.
[18]"Monitoring and validating active site redox states in protein crystals."
Antonyuk S.V., Hough M.A.
Biochim. Biophys. Acta 1814:778-784(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRFREC. JV0032.
RefSeqNP_417795.1. NC_000913.3.
YP_492096.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
1BFRX-ray2.94A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
2HTNX-ray2.50A/B/C/D/E/F/G/H1-158[»]
2VXIX-ray1.91A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
2Y3QX-ray1.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1JX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1LX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1NX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1OX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1PX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1QX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E2CX-ray1.80A/B1-158[»]
3GHQX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortalP0ABD3.
SMRP0ABD3. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36167N.
IntActP0ABD3. 2 interactions.
STRING511145.b3336.

Proteomic databases

PaxDbP0ABD3.
PRIDEP0ABD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneID12933472.
947839.
KEGGecj:Y75_p3840.
eco:b3336.
PATRIC32122104. VBIEscCol129921_3429.

Organism-specific databases

EchoBASEEB0111.
EcoGeneEG10113. bfr.

Phylogenomic databases

eggNOGCOG2193.
HOGENOMHOG000262383.
KOK03594.
OMACTRNTAV.
OrthoDBEOG6WDSKP.
PhylomeDBP0ABD3.

Enzyme and pathway databases

BioCycEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.

Gene expression databases

GenevestigatorP0ABD3.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFPIRSF002560. Bacterioferritin. 1 hit.
PRINTSPR00601. BACFERRITIN.
SUPFAMSSF47240. SSF47240. 1 hit.
TIGRFAMsTIGR00754. bfr. 1 hit.
PROSITEPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABD3.
PROP0ABD3.

Entry information

Entry nameBFR_ECOLI
AccessionPrimary (citable) accession number: P0ABD3
Secondary accession number(s): O68931, P11056, Q2M701
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene