SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O68926

- BFR_SALTY

UniProt

O68926 - BFR_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bacterioferritin

Gene
bfr, STM3443
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.

Catalytic activityi

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

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Iron 1 By similarity
Metal bindingi51 – 511Iron 1 By similarity
Metal bindingi51 – 511Iron 2 By similarity
Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partner By similarity
Metal bindingi54 – 541Iron 1 By similarity
Metal bindingi94 – 941Iron 2 By similarity
Metal bindingi127 – 1271Iron 1 By similarity
Metal bindingi127 – 1271Iron 2 By similarity
Metal bindingi130 – 1301Iron 2 By similarity

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  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

BioCyciSENT99287:GCTI-3465-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:STM3443
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158BacterioferritinPRO_0000192594Add
BLAST

Proteomic databases

PaxDbiO68926.
PRIDEiO68926.

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 By similarity.

Protein-protein interaction databases

STRINGi99287.STM3443.

Structurei

3D structure databases

ProteinModelPortaliO68926.
SMRiO68926. Positions 1-155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145Ferritin-like diironAdd
BLAST

Sequence similaritiesi

Belongs to the bacterioferritin family.

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
KOiK03594.
OMAiDHEYHES.
OrthoDBiEOG6WDSKP.
PhylomeDBiO68926.

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.

O68926-1 [UniParc]FASTAAdd to Basket

« Hide

MKGDVKIINY LNKLLGNELV AINQYFLHAR MFKNWGLTRL NDVEYHESID    50
EMKHADKYIE RILFLEGIPN LQDLGKLGIG EDVEEMLRSD LRLELEGAKD 100
LREAIAYADS VHDYVSRDMM IEILADEEGH IDWLETELDL IAKLGMQNYL 150
QSQIKVTD 158
Length:158
Mass (Da):18,355
Last modified:August 1, 1998 - v1
Checksum:i6D8145505FC59901
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF058449 Genomic DNA. Translation: AAC14283.1.
AE006468 Genomic DNA. Translation: AAL22306.1.
RefSeqiNP_462347.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL22306; AAL22306; STM3443.
GeneIDi1254966.
KEGGistm:STM3443.
PATRICi32385685. VBISalEnt20916_3640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF058449 Genomic DNA. Translation: AAC14283.1 .
AE006468 Genomic DNA. Translation: AAL22306.1 .
RefSeqi NP_462347.1. NC_003197.1.

3D structure databases

ProteinModelPortali O68926.
SMRi O68926. Positions 1-155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM3443.

Proteomic databases

PaxDbi O68926.
PRIDEi O68926.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL22306 ; AAL22306 ; STM3443 .
GeneIDi 1254966.
KEGGi stm:STM3443.
PATRICi 32385685. VBISalEnt20916_3640.

Phylogenomic databases

eggNOGi COG2193.
HOGENOMi HOG000262383.
KOi K03594.
OMAi DHEYHES.
OrthoDBi EOG6WDSKP.
PhylomeDBi O68926.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-3465-MONOMER.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002560. Bacterioferritin. 1 hit.
PRINTSi PR00601. BACFERRITIN.
SUPFAMi SSF47240. SSF47240. 1 hit.
TIGRFAMsi TIGR00754. bfr. 1 hit.
PROSITEi PS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Noorani S.M., Lindahl L., Zengel J.M.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiBFR_SALTY
AccessioniPrimary (citable) accession number: O68926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi