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Protein

Bacterioferritin

Gene

bfr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.3 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

Enzyme 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi46 – 461Iron 3PROSITE-ProRule annotation1 Publication
Metal bindingi50 – 501Iron 3PROSITE-ProRule annotation1 Publication
Metal bindingi51 – 511Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi51 – 511Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partnerPROSITE-ProRule annotation1 Publication
Metal bindingi54 – 541Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi94 – 941Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi127 – 1271Iron 1PROSITE-ProRule annotation1 Publication
Metal bindingi127 – 1271Iron 2PROSITE-ProRule annotation1 Publication
Metal bindingi130 – 1301Iron 2PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC
  3. heme binding Source: EcoCyc
  4. identical protein binding Source: EcoCyc
  5. iron ion binding Source: EcoCyc
  6. oxidoreductase activity Source: EcoliWiki

GO - Biological processi

  1. intracellular sequestering of iron ion Source: EcoCyc
  2. iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.

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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10113. bfr.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication
Mutagenesisi31 – 311M → H or L: No loss of heme binding. 1 Publication
Mutagenesisi46 – 461H → 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
Mutagenesisi50 – 501D → 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
Mutagenesisi52 – 521M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication
Mutagenesisi86 – 861M → L: No loss of heme binding. 1 Publication
Mutagenesisi127 – 1271E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication
Mutagenesisi130 – 1301H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158BacterioferritinPRO_0000192592Add
BLAST

Proteomic databases

PaxDbiP0ABD3.
PRIDEiP0ABD3.

Expressioni

Gene expression databases

GenevestigatoriP0ABD3.

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 Publications

Protein-protein interaction databases

DIPiDIP-36167N.
IntActiP0ABD3. 2 interactions.
STRINGi511145.b3336.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3430Combined sources
Helixi38 – 6427Combined sources
Helixi83 – 11028Combined sources
Helixi114 – 14431Combined sources
Helixi146 – 1527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CVPX-ray2.11A1-158[»]
4CVRX-ray1.10A1-158[»]
4CVSX-ray1.39A1-158[»]
4CVTX-ray1.79A1-158[»]
4U3GX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortaliP0ABD3.
SMRiP0ABD3. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABD3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bacterioferritin family.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
InParanoidiP0ABD3.
KOiK03594.
OMAiFLHAKMQ.
OrthoDBiEOG6WDSKP.
PhylomeDBiP0ABD3.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
PRINTSiPR00601. BACFERRITIN.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR00754. bfr. 1 hit.
PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABD3-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:158
Mass (Da):18,495
Last modified:October 25, 2005 - v1
Checksum:iA6C86CE1CD8F865A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531K → M AA sequence (PubMed:2644932).Curated

Mass spectrometryi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 73TKV → VKI in strain: ECOR 30.
Natural varianti38 – 381K → M in strain: ECOR 30.
Natural varianti57 – 571R → K in strain: ECOR 30.
Natural varianti68 – 681L → I in strain: ECOR 30.
Natural varianti78 – 781N → G in strain: ECOR 30.
Natural varianti88 – 881R → Q in strain: ECOR 30.
Natural varianti92 – 921A → R in strain: ECOR 30.
Natural varianti96 – 961D → E in strain: ECOR 30.
Natural varianti100 – 1001N → D in strain: ECOR 30.
Natural varianti106 – 1061G → A in strain: ECOR 30.
Natural varianti125 – 1251R → A in strain: ECOR 30.
Natural varianti142 – 1443QKM → GKI in strain: ECOR 30.
Natural varianti152 – 1587AQIREEG → SQIKVKD in strain: ECOR 30.

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.
PIRiJV0032. FREC.
RefSeqiNP_417795.1. NC_000913.3.
YP_492096.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneIDi12933472.
947839.
KEGGiecj:Y75_p3840.
eco:b3336.
PATRICi32122104. VBIEscCol129921_3429.

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.
PIRiJV0032. FREC.
RefSeqiNP_417795.1. NC_000913.3.
YP_492096.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CVPX-ray2.11A1-158[»]
4CVRX-ray1.10A1-158[»]
4CVSX-ray1.39A1-158[»]
4CVTX-ray1.79A1-158[»]
4U3GX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortaliP0ABD3.
SMRiP0ABD3. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36167N.
IntActiP0ABD3. 2 interactions.
STRINGi511145.b3336.

Proteomic databases

PaxDbiP0ABD3.
PRIDEiP0ABD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneIDi12933472.
947839.
KEGGiecj:Y75_p3840.
eco:b3336.
PATRICi32122104. VBIEscCol129921_3429.

Organism-specific databases

EchoBASEiEB0111.
EcoGeneiEG10113. bfr.

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
InParanoidiP0ABD3.
KOiK03594.
OMAiFLHAKMQ.
OrthoDBiEOG6WDSKP.
PhylomeDBiP0ABD3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABD3.
PROiP0ABD3.

Gene expression databases

GenevestigatoriP0ABD3.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
PRINTSiPR00601. BACFERRITIN.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR00754. bfr. 1 hit.
PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiBFR_ECOLI
AccessioniPrimary (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: March 4, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.