ID   BFD_SALTY               Reviewed;          64 AA.
AC   P0A1Z6; O68925;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Bacterioferritin-associated ferredoxin;
GN   Name=bfd; OrderedLocusNames=STM3444;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Noorani S.M., Lindahl L., Zengel J.M.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Seems to associate with BFR; could be a general redox and/or
CC       regulatory component participating in the iron storage mobilization
CC       functions of BFR. Could participate in the release or the delivery of
CC       iron from/to bacterioferritin (or other iron complexes) (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR   EMBL; AF058449; AAC14282.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22307.1; -; Genomic_DNA.
DR   RefSeq; NP_462348.1; NC_003197.2.
DR   RefSeq; WP_000289082.1; NC_003197.2.
DR   AlphaFoldDB; P0A1Z6; -.
DR   SMR; P0A1Z6; -.
DR   STRING; 99287.STM3444; -.
DR   PaxDb; P0A1Z6; -.
DR   EnsemblBacteria; AAL22307; AAL22307; STM3444.
DR   GeneID; 1254967; -.
DR   KEGG; stm:STM3444; -.
DR   PATRIC; fig|99287.12.peg.3641; -.
DR   HOGENOM; CLU_159205_3_4_6; -.
DR   OMA; MYVCLCE; -.
DR   PhylomeDB; P0A1Z6; -.
DR   BioCyc; SENT99287:STM3444-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1100; -; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   Pfam; PF04324; Fer2_BFD; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..64
FT                   /note="Bacterioferritin-associated ferredoxin"
FT                   /id="PRO_0000064917"
FT   BINDING         4
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         6
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   64 AA;  7459 MW;  D313AE29C707F64F CRC64;
     MYVCLCNGIS DKKIRQAVRQ FHPQSFQQLR KFIPVGNQCG KCIRAAREVM QDELTQMPEF
     KEIA