ID A0A2R5F167_9PROT Unreviewed; 160 AA.
AC A0A2R5F167;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
GN Name=bfr {ECO:0000313|EMBL:GBG12497.1};
GN ORFNames=NMK_0028 {ECO:0000313|EMBL:GBG12497.1};
OS Novimethylophilus kurashikiensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Novimethylophilus.
OX NCBI_TaxID=1825523 {ECO:0000313|EMBL:GBG12497.1, ECO:0000313|Proteomes:UP000245081};
RN [1] {ECO:0000313|EMBL:GBG12497.1, ECO:0000313|Proteomes:UP000245081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=La2-4 {ECO:0000313|EMBL:GBG12497.1,
RC ECO:0000313|Proteomes:UP000245081};
RX PubMed=29411502; DOI=10.1111/1462-2920.14062;
RA Lv H., Sahin N., Tani A.;
RT "Isolation and genomic characterization of Novimethylophilus kurashikiensis
RT gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of
RT Methylophilaceae.";
RL Environ. Microbiol. 20:1204-1223(2018).
CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU000623}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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:0000256|ARBA:ARBA00011713}.
CC -!- SIMILARITY: Belongs to the bacterioferritin family.
CC {ECO:0000256|ARBA:ARBA00008093, ECO:0000256|PIRNR:PIRNR002560,
CC ECO:0000256|RuleBase:RU000623}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG12497.1}.
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DR EMBL; BDOQ01000001; GBG12497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5F167; -.
DR OrthoDB; 9800505at2; -.
DR Proteomes; UP000245081; Unassembled WGS sequence.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF0; 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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR002560};
KW Iron {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|PIRSR:PIRSR002560-1};
KW Iron storage {ECO:0000256|PIRNR:PIRNR002560,
KW ECO:0000256|RuleBase:RU000623};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002560,
KW ECO:0000256|PIRSR:PIRSR002560-1};
KW Oxidoreductase {ECO:0000313|EMBL:GBG12497.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245081}.
FT DOMAIN 1..146
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
FT BINDING 18
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 52
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:0000256|PIRSR:PIRSR002560-1"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
SQ SEQUENCE 160 AA; 18808 MW; B4CE1A69359F101B CRC64;
MQGDKEVILT LNKVLKNELT AINQYFLHAR MFRNWGLEKL NDYQYKQSIR VMKEADELIE
RILFLEGLPN LQNLGKLLIG EHVVECLHGD LTYERDIQRP LLVEAIALCE RVQDYVSRDL
LEELLEHCEE AIDWLETQQT LIKDVTLPNY LQSHMEPGED
//
