ID BFRA_NEIMA Reviewed; 154 AA. AC P56998; A1IS02; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Bacterioferritin A; DE Short=BFR A; DE EC=1.16.3.1; GN Name=bfrA; OrderedLocusNames=NMA1377; OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / OS Z2491). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15465 / Z2491; RX PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A., RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., RA Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis RT Z2491."; RL Nature 404:502-506(2000). CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) CC ions, oxidizes them by dioxygen to Fe(3+), and participates in the CC subsequent Fe(3+) oxide mineral core formation within the central CC cavity of the protein complex. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000305}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron- CC binding site within each subunit is known as the ferroxidase center. CC {ECO:0000250}; CC -!- SUBUNIT: Oligomer of 24 subunits, arranged as 12 dimers, that are CC packed together to form an approximately spherical molecule with a CC central cavity, in which large amounts of iron can be deposited. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}. 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; AL157959; CAM08550.1; -; Genomic_DNA. DR PIR; C81907; C81907. DR RefSeq; WP_002222445.1; NC_003116.1. DR AlphaFoldDB; P56998; -. DR SMR; P56998; -. DR EnsemblBacteria; CAM08550; CAM08550; NMA1377. DR GeneID; 61281377; -. DR KEGG; nma:NMA1377; -. DR HOGENOM; CLU_104506_2_0_4; -. DR Proteomes; UP000000626; Chromosome. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR CDD; cd00907; Bacterioferritin; 1. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR012347; Ferritin-like. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR008331; Ferritin_DPS_dom. DR NCBIfam; TIGR00754; bfr; 1. DR PANTHER; PTHR30295; BACTERIOFERRITIN; 1. DR PANTHER; PTHR30295:SF9; BACTERIOFERRITIN; 1. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF002560; Bacterioferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 3: Inferred from homology; KW Heme; Iron; Iron storage; Metal-binding; Oxidoreductase. FT CHAIN 1..154 FT /note="Bacterioferritin A" FT /id="PRO_0000192603" FT DOMAIN 1..145 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 18 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 48 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_note="ligand shared between dimeric partners" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 93 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" SQ SEQUENCE 154 AA; 17947 MW; 63C80610DDA4346E CRC64; MQGNQAVVDY MNELLSGELA ARDQYFIHSR LYSEWGYTKL FERLNHEMEE ETTHAEDFIR RILMLGGTPK MARAELNIGT DVVSCLKADL QTEYEVRDAL KKGIKLCEEA QDYVSRDLMV AQLKDTEEDH AHWLEQQLRL IELIGEGNYY QSQL //