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Database: UniProt
Entry: E3I8J2_RHOVT
LinkDB: E3I8J2_RHOVT
Original site: E3I8J2_RHOVT 
ID   E3I8J2_RHOVT            Unreviewed;        69 AA.
AC   E3I8J2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN   OrderedLocusNames=Rvan_1651 {ECO:0000313|EMBL:ADP70901.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS   4299).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70901.1, ECO:0000313|Proteomes:UP000001399};
RN   [1] {ECO:0000313|Proteomes:UP000001399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC   {ECO:0000313|Proteomes:UP000001399};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; CP002292; ADP70901.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3I8J2; -.
DR   STRING; 648757.Rvan_1651; -.
DR   KEGG; rva:Rvan_1651; -.
DR   eggNOG; COG2906; Bacteria.
DR   HOGENOM; CLU_159205_0_1_5; -.
DR   OrthoDB; 7428628at2; -.
DR   Proteomes; UP000001399; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..50
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   69 AA;  7550 MW;  0B1A91B49F23982A CRC64;
     MIICSCNVLS DEAVRSAMSS PNPPRTPCQV HRHFGCTAKC GRCTRSLRDA MDDGRAEQPM
     EQMPVAKVA
//
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