ID J1ZSK1_9ACTN Unreviewed; 91 AA.
AC J1ZSK1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN ORFNames=SU9_008475 {ECO:0000313|EMBL:QTZ91509.1}, SU9_23035
GN {ECO:0000313|EMBL:EJJ04591.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ04591.1};
RN [1] {ECO:0000313|EMBL:EJJ04591.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ04591.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91509.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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; AJGV01000139; EJJ04591.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91509.1; -; Genomic_DNA.
DR RefSeq; WP_006606120.1; NZ_CP072931.1.
DR AlphaFoldDB; J1ZSK1; -.
DR STRING; 1160718.SU9_23035; -.
DR KEGG; sauh:SU9_008475; -.
DR PATRIC; fig|1160718.3.peg.4658; -.
DR eggNOG; COG2906; Bacteria.
DR HOGENOM; CLU_159205_1_0_11; -.
DR OrthoDB; 9815350at2; -.
DR Proteomes; UP000009036; 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:UP000009036};
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 91 AA; 9332 MW; 17B06956C2A06834 CRC64;
MYVCSCFGIT EQQVREHADT GACTPRQIAS ACKAGTDCGN CVRRIQALLG RGACPRRELI
ENGASEPLGG VSEPLAAAAG AVEPVVLSEA A
//