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Database: UniProt
Entry: A0A2S2CWF3_9PROT
LinkDB: A0A2S2CWF3_9PROT
Original site: A0A2S2CWF3_9PROT 
ID   A0A2S2CWF3_9PROT        Unreviewed;       159 AA.
AC   A0A2S2CWF3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
GN   Name=bfr {ECO:0000313|EMBL:AWK88788.1};
GN   ORFNames=DEW08_22185 {ECO:0000313|EMBL:AWK88788.1};
OS   Azospirillum thermophilum.
OG   Plasmid unnamed1 {ECO:0000313|EMBL:AWK88788.1,
OG   ECO:0000313|Proteomes:UP000245629}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88788.1, ECO:0000313|Proteomes:UP000245629};
RN   [1] {ECO:0000313|Proteomes:UP000245629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RC   PLASMID=unnamed1 {ECO:0000313|Proteomes:UP000245629};
RA   Zhao Z.;
RT   "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00037326}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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; CP029356; AWK88788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2CWF3; -.
DR   KEGG; azz:DEW08_22185; -.
DR   OrthoDB; 9800505at2; -.
DR   Proteomes; UP000245629; Plasmid unnamed1.
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: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 {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}; Plasmid {ECO:0000313|EMBL:AWK88788.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245629}.
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         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         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         131
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;  18321 MW;  A7E5E80F30A58D66 CRC64;
     MQGDPGVIDR LNKLLIGELS AADQYLAHAS MMENWGFKAI YERIAHERHD ELEHADKLIK
     RILFLEGTPD VASRDPLRIG KDIPEMLRND LTLELEVVDA LKEAIAYCEQ VRDYDTRRIL
     VELLEDTEED HAHWLEQQLT LINMIGLQNY LQSAIGKLT
//
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