Ferritin BfrB - Mycobacterium tuberculosis

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P96237 (BFRB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ferritin BfrB
EC=1.16.3.1

Alternative name(s):
Non-heme ferritin Ftn
Nox19

Gene names

Name:	bfrB
Synonyms:	ftn
Ordered Locus Names:	Rv3841, MT3949

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe²⁺ ions into Fe³⁺ ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex. Ref.9
Catalytic activity	4 Fe²⁺ + 4 H⁺ + O₂ = 4 Fe³⁺ + 2 H₂O. Ref.9
Subunit structure	Homooligomer of 24 subunits that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be stored. Ref.9
Induction	Induced by 1 mM reactive nitrogen intermediate sodium nitroprusside dihydrate (at protein level). Induced by exposure to 50 µM FeCl₃. A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia), repressed by carbon monoxide (CO). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. Ref.3 Ref.4 Ref.5
Sequence similarities	Belongs to the ferritin family. Prokaryotic subfamily. Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
Biological process	Iron storage
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular sequestering of iron ion Inferred from direct assay Ref.9. Source: MTBBASE iron assimilation by chelation and transport Traceable author statement. Source: Reactome iron ion transport Inferred from electronic annotation. Source: InterPro protein homooligomerization Inferred from physical interaction Ref.8 Ref.9. Source: MTBBASE response to host immune response Traceable author statement. Source: Reactome response to hypoxia Inferred from direct assay Ref.5. Source: MTBBASE response to nitrosative stress Inferred from expression pattern Ref.3. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE extracellular region Inferred from direct assay PubMed 17443846. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352 PubMed 15525680. Source: MTBBASE
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from direct assay Ref.9. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 181

180

Ferritin BfrB

PRO_0000392942

Regions

Domain

5 – 150

146

Ferritin-like diiron

Sites

Metal binding

Iron 1 By similarity

Metal binding

Iron 1 By similarity

Metal binding

Iron 2 By similarity

Metal binding

Iron 1 By similarity

Metal binding

Iron 2 By similarity

Metal binding

132

Iron 2 By similarity

Secondary structure

181

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P96237 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C0F375669A292F55
Show »

FASTA

181

20,442

        10         20         30         40         50         60 
MTEYEGPKTK FHALMQEQIH NEFTAAQQYV AIAVYFDSED LPQLAKHFYS QAVEERNHAM 

        70         80         90        100        110        120 
MLVQHLLDRD LRVEIPGVDT VRNQFDRPRE ALALALDQER TVTDQVGRLT AVARDEGDFL 

       130        140        150        160        170        180 
GEQFMQWFLQ EQIEEVALMA TLVRVADRAG ANLFELENFV AREVDVAPAA SGAPHAAGGR 


L

« Hide

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. 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. 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]	"Response to reactive nitrogen intermediates in Mycobacterium tuberculosis: induction of the 16-kilodalton alpha-crystallin homolog by exposure to nitric oxide donors." Garbe T.R., Hibler N.S., Deretic V. Infect. Immun. 67:460-465(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17, INDUCTION BY NITRIC OXIDE STRESS. Strain: ATCC 25618 / H37Rv and I2646.
[4]	"Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin." Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I., Schoolnik G.K. Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY HYPOXIA. Strain: ATCC 25618 / H37Rv.
[5]	"Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins." Rosenkrands I., Slayden R.A., Crawford J., Aagaard C., Barry C.E. III, Andersen P. J. Bacteriol. 184:3485-3491(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY HYPOXIA. Strain: ATCC 25618 / H37Rv.
[6]	"IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response." Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I. Infect. Immun. 70:3371-3381(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCED BY IRON. Strain: ATCC 25618 / H37Rv.
[7]	"Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection." Shiloh M.U., Manzanillo P., Cox J.S. Cell Host Microbe 3:323-330(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REPRESSION BY CARBON MONOXIDE (CO). Strain: ATCC 35801 / TMC 107 / Erdman.
[8]	"Crystallization and preliminary X-ray crystallographic analysis of a Mycobacterium tuberculosis ferritin homolog, BfrB." McMath L.M., Habel J.E., Sankaran B., Yu M., Hung L.W., Goulding C.W. Acta Crystallogr. F 66:1657-1661(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION. Strain: ATCC 25618 / H37Rv.
[9]	"Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended C-terminus involved in ferroxidase activity." Khare G., Gupta V., Nangpal P., Gupta R.K., Sauter N.K., Tyagi A.K. PLoS ONE 6:E18570-E18570(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF102693 Genomic DNA. Translation: AAF06357.1.
AE000516 Genomic DNA. Translation: AAK48316.1.
BX842584 Genomic DNA. Translation: CAB06225.1.
AL123456 Genomic DNA. Translation: CCP46670.1.

PIR

F70653.

RefSeq

NP_218358.1. NC_000962.3.
NP_338502.1. NC_002755.2.
YP_006517338.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QD8	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X	1-181	[»]
3UNO	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X	1-181	[»]

ProteinModelPortal

P96237.

SMR

P96237. Positions 8-181.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv3841.

Proteomic databases

PaxDb

P96237.

PRIDE

P96237.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK48316; AAK48316; MT3949.

GeneID

13317465.
886176.
926311.

KEGG

mtc:MT3949.
mtu:Rv3841.
mtv:RVBD_3841.

PATRIC

18130439. VBIMycTub22151_4307.

Organism-specific databases

TubercuList

Rv3841.

Phylogenomic databases

eggNOG

COG1528.

HOGENOM

HOG000223382.

OMA

QYFLDRD.

ProtClustDB

CLSK872257.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Family and domain databases

Gene3D

1.20.1260.10. 1 hit.

InterPro

IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]

PANTHER

PTHR11431. PTHR11431. 1 hit.

Pfam

PF00210. Ferritin. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BFRB_MYCTU

Accession

Primary (citable) accession number: P96237
Secondary accession number(s): L0TGW6, Q7BS08, Q7D4R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents