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Database: UniProt
Entry: A0A119CY05_THIDE
LinkDB: A0A119CY05_THIDE
Original site: A0A119CY05_THIDE 
ID   A0A119CY05_THIDE        Unreviewed;       149 AA.
AC   A0A119CY05;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Ferric uptake regulation protein {ECO:0000256|ARBA:ARBA00020910, ECO:0000256|RuleBase:RU364037};
GN   Name=fur {ECO:0000256|RuleBase:RU364037};
GN   ORFNames=ABW22_02165 {ECO:0000313|EMBL:KVW99064.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW99064.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW99064.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW99064.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602481-2};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602481-2};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR602481-2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602481-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR602481-1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU364037}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU364037}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000256|ARBA:ARBA00007957,
CC       ECO:0000256|RuleBase:RU364037}.
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:KVW99064.1}.
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DR   EMBL; LDUG01000007; KVW99064.1; -; Genomic_DNA.
DR   RefSeq; WP_059751559.1; NZ_LDUG01000007.1.
DR   AlphaFoldDB; A0A119CY05; -.
DR   STRING; 1123392.GCA_000376425_01236; -.
DR   PATRIC; fig|36861.3.peg.3280; -.
DR   eggNOG; COG0735; Bacteria.
DR   OrthoDB; 8659436at2; -.
DR   Proteomes; UP000064243; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07153; Fur_like; 1.
DR   Gene3D; 3.30.1490.190; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002481; FUR.
DR   InterPro; IPR043135; Fur_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR33202:SF2; FERRIC UPTAKE REGULATION PROTEIN; 1.
DR   PANTHER; PTHR33202; ZINC UPTAKE REGULATION PROTEIN; 1.
DR   Pfam; PF01475; FUR; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364037};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364037};
KW   Iron {ECO:0000256|PIRSR:PIRSR602481-2, ECO:0000256|RuleBase:RU364037};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602481-1,
KW   ECO:0000256|RuleBase:RU364037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW   Repressor {ECO:0000256|RuleBase:RU364037};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364037};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364037};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602481-1}.
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
SQ   SEQUENCE   149 AA;  17281 MW;  324238BE7D65A1EC CRC64;
     MSHPSDLKSI GLKATLPRLK ILELFEQSHK RHMTAEEVYR LLSDEGQDIG LATVYRVLTQ
     FEQAGLLIRH HFDSDKAVFE LNQGEHHDHL VCLQCGKVEE FFDAEIEKRQ TRIAKERGFS
     IHDHSLHIYA DCIKENCPNR KPGDNRHRA
//
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