ID A0A1Q4WMM9_9ACTN Unreviewed; 159 AA.
AC A0A1Q4WMM9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
DE EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN ORFNames=AMK13_02345 {ECO:0000313|EMBL:OKI11285.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI11285.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI11285.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI11285.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:0000256|PIRNR:PIRNR002560}.
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 Evidence={ECO:0000256|PIRNR:PIRNR002560};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: Homooligomer 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:ARBA00011637}.
CC -!- SIMILARITY: Belongs to the bacterioferritin family.
CC {ECO:0000256|PIRNR:PIRNR002560, 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:OKI11285.1}.
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DR EMBL; LIPD01000001; OKI11285.1; -; Genomic_DNA.
DR RefSeq; WP_049655380.1; NZ_LIPD01000001.1.
DR AlphaFoldDB; A0A1Q4WMM9; -.
DR OrthoDB; 9800505at2; -.
DR Proteomes; UP000186379; Unassembled WGS sequence.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000186379}.
FT DOMAIN 1..145
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 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 51
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 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
SQ SEQUENCE 159 AA; 18598 MW; 1B622CC272BED03C CRC64;
MQGDPEVIEF LNEQLTAELT AINQYFLHAK MQENFGWTKL AKYTRHESFD EMKHAETLTD
RILFLEGLPN YQRLFHVRIG QTVKEMFEAD RQIEVEAIDR LKRGIVVMRA KNDVTSANIF
EDILADEEHH IDYLDTQLEL LEKLGEALYL ATVIEQPES
//