P63697 (BFR_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bacterioferritin
Short name=BFR
EC=1.16.3.1

Gene names

Name:	bfr
Synonyms:	bfrA
Ordered Locus Names:	Rv1876, MT1925
ORF Names:	MTCY180.42c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.3 Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.
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. Ref.4
Sequence similarities	Belongs to the bacterioferritin family. Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
Biological process	Iron storage
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	iron assimilation by chelation and transport Traceable author statement. Source: Reactome iron ion transport Inferred from electronic annotation. Source: InterPro response to host immune response Traceable author statement. Source: Reactome response to iron ion Inferred from expression pattern PubMed 11722747. Source: MTBBASE
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular region Inferred from direct assay PubMed 17443846. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352. Source: MTBBASE
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 159

159

Bacterioferritin

PRO_0000192600

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); shared with dimeric partner By similarity

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

159

Helix Strand Turn

Details...

Helix

5 – 34

30

Helix

38 – 64

27

Helix

83 – 110

28

Helix

114 – 144

31

Helix

146 – 151

6

Sequences

	Sequence		Length	Mass (Da)
	P63697 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 098B6D7392A9CD60	FASTA	159	18,341
	10 20 30 40 50 60 MQGDPDVLRL LNEQLTSELT AINQYFLHSK MQDNWGFTEL AAHTRAESFD EMRHAEEITD 70 80 90 100 110 120 RILLLDGLPN YQRIGSLRIG QTLREQFEAD LAIEYDVLNR LKPGIVMCRE KQDTTSAVLL 130 140 150 EKIVADEEEH IDYLETQLEL MDKLGEELYS AQCVSRPPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of bacterioferritin A from Mycobacterium tuberculosis." Gupta V., Gupta R.K., Khare G., Salunke D.M., Tyagi A.K. Acta Crystallogr. F 64:398-401(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION, HEME-BINDING. Strain: ATCC 25618 / H37Rv.
[4]	"Crystal structure of Bfr A from Mycobacterium tuberculosis: incorporation of selenomethionine results in cleavage and demetallation of haem." Gupta V., Gupta R.K., Khare G., Salunke D.M., Tyagi A.K. PLoS ONE 4:E8028-E8028(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH IRON IONS AND A DEGRADED PORPHYRIN DERIVATIVE, SUBUNIT. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000516 Genomic DNA. Translation: AAK46197.1.
AL123456 Genomic DNA. Translation: CCP44642.1.

PIR

A70515.

RefSeq

NP_216392.1. NC_000962.3.
NP_336383.1. NC_002755.2.
YP_006515276.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WTL	X-ray	2.59	A/B/C/D/E/F	1-159	[»]
3QB9	X-ray	2.11	A/B/C/D/E/F	1-159	[»]
3UOF	X-ray	2.90	A/B/C/D/E/F	1-159	[»]
3UOI	X-ray	1.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x	1-159	[»]

ProteinModelPortal

P63697.

SMR

P63697. Positions 1-159.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv1876.

Proteomic databases

PaxDb

P63697.

PRIDE

P63697.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK46197; AAK46197; MT1925.

GeneID

13316667.
885767.
923656.

KEGG

mtc:MT1925.
mtu:Rv1876.

PATRIC

18125997. VBIMycTub22151_2111.

Organism-specific databases

TubercuList

Rv1876.

Phylogenomic databases

eggNOG

COG2193.

HOGENOM

HOG000262383.

KO

K03594.

OMA

HHIDFLE.

ProtClustDB

CLSK791451.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Family and domain databases

Gene3D

1.20.1260.10. 1 hit.

InterPro

IPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

PIRSF

PIRSF002560. Bacterioferritin. 1 hit.

PRINTS

PR00601. BACFERRITIN.

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

TIGRFAMs

TIGR00754. bfr. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P63697.

Entry information

Entry name

BFR_MYCTU

Accession

Primary (citable) accession number: P63697
Secondary accession number(s): L0T7Y6, O08465

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 29, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program