P24602 (BFR_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bacterioferritin
Short name=BFR
EC=1.16.3.1

Gene names

Name:	bfr
Ordered Locus Names:	sll1341

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	156 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.
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer Potential. Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center By similarity.
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 By similarity.
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	Complete proteome Direct protein sequencing Reference proteome
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
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 156	156	Bacterioferritin		PRO_0000192613
Regions
	Domain	1 – 146	146	Ferritin-like diiron
Sites
	Metal binding	18	1	Iron 1 By similarity
	Metal binding	48	1	Iron (heme axial ligand); shared with dimeric partner Potential
	Metal binding	51	1	Iron 1 By similarity
	Metal binding	51	1	Iron 2 By similarity
	Metal binding	54	1	Iron 1 By similarity
	Metal binding	94	1	Iron 2 By similarity
	Metal binding	128	1	Iron 1 By similarity
	Metal binding	128	1	Iron 2 By similarity
	Metal binding	131	1	Iron 2 By similarity
Experimental info
	Sequence conflict	53 – 54	2	AH → HA AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P24602 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 7C1A13B31157AF86	FASTA	156	18,331
	10 20 30 40 50 60 MKGKPAVLAQ LHKLLRGELA ARDQYFIHSR MYQDWGLEKL YSRIDHEMQD ETAHASLLIE 70 80 90 100 110 120 RILFLEETPD LSQQDPIRVG KTVPEMLQYD LDYEYEVIAN LKEAMAVCEQ EQDYQSRDLL 130 140 150 LKILADTEED HAYWLEKQLG LIEKIGLQNY LQSQMS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[2]	"Purification, characterization and function of bacterioferritin from the cyanobacterium Synechocystis P.C.C. 6803." Laulhere J.-P., Laboure A.-M., van Wuytswinkel O., Gagnon J., Briat J.-F. Biochem. J. 281:785-793(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-54.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA18637.1.
PIR	S76725.
RefSeq	NP_442825.1. NC_000911.1. YP_005652886.1. NC_017277.1. YP_007452701.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P24602.
ModBase	Search...
Protein-protein interaction databases
STRING	1148.sll1341.
Proteomic databases
PaxDb	P24602.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA18637; BAA18637; BAA18637.
GeneID	12255164. 14618385. 952063.
KEGG	syn:sll1341. syy:SYNGTS_2933.
PATRIC	23843424. VBISynSp132158_3248.
Phylogenomic databases
eggNOG	COG2193.
HOGENOM	HOG000262383.
KO	K03594.
OMA	HSIHAEI.
ProtClustDB	CLSK2301948.
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...

Entry information

Entry name

BFR_SYNY3

Accession

Primary (citable) accession number: P24602
Secondary accession number(s): P74531

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program