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Database: UniProt
Entry: E3HPC7_ACHXA
LinkDB: E3HPC7_ACHXA
Original site: E3HPC7_ACHXA 
ID   E3HPC7_ACHXA            Unreviewed;       158 AA.
AC   E3HPC7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
GN   Name=bfr {ECO:0000313|EMBL:ADP13506.1};
GN   OrderedLocusNames=AXYL_00144 {ECO:0000313|EMBL:ADP13506.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP13506.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP13506.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP13506.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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}.
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DR   EMBL; CP002287; ADP13506.1; -; Genomic_DNA.
DR   RefSeq; WP_013390908.1; NC_014640.1.
DR   AlphaFoldDB; E3HPC7; -.
DR   STRING; 762376.AXYL_00144; -.
DR   GeneID; 84694691; -.
DR   KEGG; axy:AXYL_00144; -.
DR   eggNOG; COG2193; Bacteria.
DR   HOGENOM; CLU_104506_2_0_4; -.
DR   OrthoDB; 9800505at2; -.
DR   Proteomes; UP000006876; Chromosome.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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}.
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         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         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
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   158 AA;  18240 MW;  E95CCF9513DA1C40 CRC64;
     MKGDKTVIQF LNKQLTNELT AINQYFLHAR MLNHWGFDKL GKHEYEESIG EMKHADRLIA
     RIFMLDGLPN LQDLHKLLIG EDVPELLACD LKLEQGAQAT VKEAIAHCES VRDYVSRDLF
     QDILDDTEEH IDYLETQIDL IDKVGIQNYL QSQMSVPE
//
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