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Database: UniProt
Entry: Q57J28_SALCH
LinkDB: Q57J28_SALCH
Original site: Q57J28_SALCH 
ID   Q57J28_SALCH            Unreviewed;        64 AA.
AC   Q57J28;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN   Name=bfd {ECO:0000313|EMBL:AAX67284.1};
GN   OrderedLocusNames=SCH_3378 {ECO:0000313|EMBL:AAX67284.1};
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX67284.1, ECO:0000313|Proteomes:UP000000538};
RN   [1] {ECO:0000313|EMBL:AAX67284.1, ECO:0000313|Proteomes:UP000000538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67 {ECO:0000313|EMBL:AAX67284.1,
RC   ECO:0000313|Proteomes:UP000000538};
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA   Lee Y.S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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).
CC       {ECO:0000256|ARBA:ARBA00037130}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; AE017220; AAX67284.1; -; Genomic_DNA.
DR   RefSeq; WP_000289082.1; NC_006905.1.
DR   AlphaFoldDB; Q57J28; -.
DR   SMR; Q57J28; -.
DR   KEGG; sec:SCH_3378; -.
DR   HOGENOM; CLU_159205_3_4_6; -.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd19945; Fer2_BFD; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   PANTHER; PTHR37424; BACTERIOFERRITIN-ASSOCIATED FERREDOXIN; 1.
DR   PANTHER; PTHR37424:SF1; BACTERIOFERRITIN-ASSOCIATED FERREDOXIN; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..51
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   64 AA;  7459 MW;  D313AE29C707F64F CRC64;
     MYVCLCNGIS DKKIRQAVRQ FHPQSFQQLR KFIPVGNQCG KCIRAAREVM QDELTQMPEF
     KEIA
//
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