ID A0A1Q4W527_9ACTN Unreviewed; 107 AA.
AC A0A1Q4W527;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN ORFNames=A6A06_11210 {ECO:0000313|EMBL:OKI05196.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI05196.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI05196.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI05196.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKI05196.1}.
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DR EMBL; LWKZ01000012; OKI05196.1; -; Genomic_DNA.
DR RefSeq; WP_073762216.1; NZ_LWKZ01000012.1.
DR AlphaFoldDB; A0A1Q4W527; -.
DR STRING; 1718985.A6A06_11210; -.
DR OrthoDB; 9815350at2; -.
DR Proteomes; UP000185893; Unassembled WGS sequence.
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:UP000185893};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..50
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT REGION 58..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 107 AA; 11025 MW; 564C6E9E536D6060 CRC64;
MYVCSCFGIT EQQVREHAES GACTPRQIAS ASKAGTDCGG CVRRIQALLG RGTCPRRELI
DQGAPEPLGA EPSDEAAAGT DAGTRVPYDI TPHATPDAMP GALPEAA
//
