Reviewed, UniProtKB/Swiss-Prot P0ABD3 (BFR_ECOLI)

Names and origin

Protein names

Recommended name:
    Bacterioferritin
      Short name=BFR
Alternative name(s):
    Cytochrome b-1
    Cytochrome b-557

Gene names

Name:	bfr
Ordered Locus Names:	b3336, JW3298

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May perform analogous functions in iron detoxification and storage to that of animal ferritins.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer.
Subunit structure	Oligomer of 24 identical subunits.
Miscellaneous	The di-iron binding site functions as active site where iron ions are oxidized from Fe2+ to Fe3+ before they are stored.
Sequence similarities	Belongs to the bacterioferritin family. Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
Biological process	Iron storage
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW iron ion transport Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ferric iron binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 158

158

Bacterioferritin

PRO_0000192592

Regions

Domain

1 – 145

145

Ferritin-like diiron

Sites

Metal binding

18

1

Iron 1

Metal binding

51

1

Iron 1

Metal binding

51

1

Iron 2

Metal binding

52

1

Iron (heme axial ligand)

Metal binding

54

1

Iron 1

Metal binding

94

1

Iron 2

Metal binding

127

1

Iron 1

Metal binding

127

1

Iron 2

Metal binding

130

1

Iron 2

Natural variations

Natural variant

5 – 7

3

TKV → VKI in strain: ECOR 30.

Natural variant

38

1

K → M in strain: ECOR 30.

Natural variant

57

1

R → K in strain: ECOR 30.

Natural variant

68

1

L → I in strain: ECOR 30.

Natural variant

78

1

N → G in strain: ECOR 30.

Natural variant

88

1

R → Q in strain: ECOR 30.

Natural variant

92

1

A → R in strain: ECOR 30.

Natural variant

96

1

D → E in strain: ECOR 30.

Natural variant

100

1

N → D in strain: ECOR 30.

Natural variant

106

1

G → A in strain: ECOR 30.

Natural variant

125

1

R → A in strain: ECOR 30.

Natural variant

142 – 144

3

QKM → GKI in strain: ECOR 30.

Natural variant

152 – 158

7

AQIREEG → SQIKVKD in strain: ECOR 30.

Experimental info

Sequence conflict

53

1

K → M AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

158

Helix Strand Turn

Details...

Helix

5 – 35

31

Helix

38 – 64

27

Helix

83 – 111

29

Helix

114 – 144

31

Helix

146 – 151

6

Sequences

	Sequence		Length	Mass (Da)
	P0ABD3-1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: A6C86CE1CD8F865A	FASTA	158	18,495
	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

References

	« Hide 'large scale' referencesShow '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: 2661540] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 2644932] [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: 7959070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158. Strain: K12.
[7]	"Structure of a monoclinic crystal from 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: 9867433] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS).
[8]	"Structure of a unique twofold symmetric haem-binding site." Frolow F., Kalb A.J., Yariv J. Nat. Struct. Biol. 1:453-460(1994) [PubMed: 7664064] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

FREC. JV0032.

RefSeq

AP_004454.1.
NP_417795.1.

3D structure databases

PDBPDBe

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	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0ABD3.

2-D gel databases

ECO2DBASE

C014.3. 6TH EDITION.

Genome annotation databases

GeneID

947839.

GenomeReviews

Gene locus JW3298 in contig AP009048_GR.
Gene locus b3336 in contig U00096_GR.

KEGG

ecj:JW3298.
eco:b3336.

Organism-specific databases

EchoBASE

EB0111.

EcoGene

EG10113. bfr.

CMR

Search...

Phylogenomic databases

HOGENOM

HBG288894.

OMA

FLDGFPN.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10113-MON.
ECOL168927:B3336-MON.

Gene expression databases

Genevestigator

P0ABD3.

Family and domain databases

InterPro

IPR002024. Bacterioferritin.
IPR009040. Ferritin-like.
IPR009078. Ferritin/RR-like.
IPR008331. Ferritin_Dps.
IPR012347. Ferritin_rel.
[Graphical view]

Gene3D

G3DSA:1.20.1260.10. Ferritin_rel. 1 hit.

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

PIRSF

PIRSF002560. Bacterioferritin. 1 hit.

PRINTS

PR00601. BACFERRITIN.

PROSITE

PS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BFR_ECOLI

Accession

Primary (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:	December 15, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)