ID F6ELF2_HOYSD Unreviewed; 219 AA.
AC F6ELF2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Diphtheria toxin repressor {ECO:0000256|ARBA:ARBA00016140};
DE AltName: Full=Iron-dependent diphtheria tox regulatory element {ECO:0000256|ARBA:ARBA00032618};
DE AltName: Full=Tox regulatory factor {ECO:0000256|ARBA:ARBA00033329};
GN OrderedLocusNames=AS9A_1753 {ECO:0000313|EMBL:AEF40202.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40202.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF40202.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DtxR/MntR family.
CC {ECO:0000256|ARBA:ARBA00007871}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002786; AEF40202.1; -; Genomic_DNA.
DR AlphaFoldDB; F6ELF2; -.
DR STRING; 443218.AS9A_1753; -.
DR KEGG; asd:AS9A_1753; -.
DR eggNOG; COG1321; Bacteria.
DR HOGENOM; CLU_069532_0_0_11; -.
DR Proteomes; UP000009235; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR Gene3D; 2.30.30.90; -; 1.
DR Gene3D; 1.10.60.10; Iron dependent repressor, metal binding and dimerisation domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR040767; DtxR_SH3.
DR InterPro; IPR007167; Fe-transptr_FeoA.
DR InterPro; IPR001367; Fe_dep_repressor.
DR InterPro; IPR036421; Fe_dep_repressor_sf.
DR InterPro; IPR038157; FeoA_core_dom.
DR InterPro; IPR022687; HTH_DTXR.
DR InterPro; IPR022689; Iron_dep_repressor.
DR InterPro; IPR008988; Transcriptional_repressor_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33238; IRON (METAL) DEPENDENT REPRESSOR, DTXR FAMILY; 1.
DR PANTHER; PTHR33238:SF10; IRON-DEPENDENT REPRESSOR IDER; 1.
DR Pfam; PF18357; DtxR; 1.
DR Pfam; PF02742; Fe_dep_repr_C; 1.
DR Pfam; PF01325; Fe_dep_repress; 1.
DR SMART; SM00899; FeoA; 1.
DR SMART; SM00529; HTH_DTXR; 1.
DR SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR SUPFAM; SSF47979; Iron-dependent repressor protein, dimerization domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50944; HTH_DTXR; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..56
FT /note="HTH dtxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50944"
SQ SEQUENCE 219 AA; 24467 MW; 87EEE6FD3BBDD7C8 CRC64;
MYLRTVYELE EEGVVPLRAR IAERLDQSGP TVSQTVARME RDGLLSVAGD RHLELTPKGR
ELAVAVMRKH RLAERLLVDV IGLKWENVHA EACRWEHVMS EDVERRLVSV LNHPTTSPYG
NPIPGLEMLG LDLPFEQEPA LIRLSDIPQG TSVHVMIRRL AEHVQVDTEL IARLRHAGVV
PNARITAQAY PGGIRITTPG HEGLDISDDM AHAIQVEKV
//
