ID BFR_RHOCA Reviewed; 161 AA. AC Q59738; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 02-MAR-2010, entry version 56. DE RecName: Full=Bacterioferritin; DE Short=BFR; GN Name=bfr; OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 938 / 37b4; RX MEDLINE=96275893; PubMed=8674981; DOI=10.1016/0378-1097(96)00133-4; RA Penfold C.N., Ringeling P.L., Davy S.L., Moore G.R., McEwan A.G., RA Spiro S.; RT "Isolation, characterisation and expression of the bacterioferritin RT gene of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 139:143-148(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=21620770; PubMed=11752777; RA Cobessi D., Huang L.-S., Ban M., Pon N.G., Daldal F., Berry E.A.; RT "The 2.6 A resolution structure of Rhodobacter capsulatus RT bacterioferritin with metal-free dinuclear site and heme iron in a RT crystallographic 'special position'."; RL Acta Crystallogr. D 58:29-38(2002). CC -!- FUNCTION: May perform analogous functions in iron detoxification CC and storage to that of animal ferritins (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer. CC -!- SUBUNIT: Oligomer of 24 identical subunits. CC -!- MISCELLANEOUS: The di-iron binding site functions as active site CC where iron ions are oxidized from Fe(2+) to Fe(3+) before they are CC stored. CC -!- SIMILARITY: Belongs to the bacterioferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z54247; CAA91017.1; -; Genomic_DNA. DR PIR; S48182; S48182. DR PDB; 1JGC; X-ray; 2.60 A; A/B/C=1-161. DR PDBsum; 1JGC; -. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:InterPro. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR009040; Ferritin-like. DR InterPro; IPR009078; Ferritin/RR-like. DR InterPro; IPR008331; Ferritin_Dps. DR InterPro; IPR012347; Ferritin_rel. DR Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF002560; Bacterioferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR SUPFAM; SSF47240; Ferritin/RR_like; 1. DR TIGRFAMs; TIGR00754; bfr; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Iron storage; Metal-binding. FT CHAIN 1 161 Bacterioferritin. FT /FTId=PRO_0000192611. FT DOMAIN 1 145 Ferritin-like diiron. FT METAL 18 18 Iron 1. FT METAL 51 51 Iron 1. FT METAL 51 51 Iron 2. FT METAL 52 52 Iron (heme axial ligand). FT METAL 54 54 Iron 1. FT METAL 94 94 Iron 2. FT METAL 127 127 Iron 1. FT METAL 127 127 Iron 2. FT METAL 130 130 Iron 2. FT HELIX 5 34 FT HELIX 38 64 FT HELIX 83 111 FT HELIX 114 144 FT HELIX 146 152 SQ SEQUENCE 161 AA; 18173 MW; 9E534CBC531EC709 CRC64; MKGDAKVIEF LNAALRSELT AISQYWVHFR LQEDWGLAKM AKKSREESIE EMGHADKIIA RILFLEGHPN LQKLDPLRIG EGPRETLECD LAGEHDALKL YREARDYCAE VGDIVSKNIF ESLITDEEGH VDFLETQISL YDRLGPQGFA LLNAAPMDAA E //