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Database: UniProt
Entry: W1DGT1_KLEPN
LinkDB: W1DGT1_KLEPN
Original site: W1DGT1_KLEPN 
ID   W1DGT1_KLEPN            Unreviewed;       150 AA.
AC   W1DGT1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Ferric uptake regulation protein {ECO:0000256|ARBA:ARBA00020910, ECO:0000256|RuleBase:RU364037};
GN   Name=fur {ECO:0000256|RuleBase:RU364037};
OS   Klebsiella pneumoniae IS43.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL08663.1, ECO:0000313|Proteomes:UP000019183};
RN   [1] {ECO:0000313|EMBL:CDL08663.1, ECO:0000313|Proteomes:UP000019183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS43 {ECO:0000313|EMBL:CDL08663.1,
RC   ECO:0000313|Proteomes:UP000019183};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the General
RT   Hospital Vienna.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a global negative controlling element, employing
CC       Fe(2+) as a cofactor to bind the operator of the repressed genes.
CC       Regulates the expression of several outer-membrane proteins including
CC       the iron transport operon. {ECO:0000256|ARBA:ARBA00037693}.
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:CDL08663.1}.
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DR   EMBL; CBWK010000231; CDL08663.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1DGT1; -.
DR   SMR; W1DGT1; -.
DR   eggNOG; COG0735; Bacteria.
DR   Proteomes; UP000019183; 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}; 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         87
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         89
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-2"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
SQ   SEQUENCE   150 AA;  17109 MW;  AA7ECC67D0D51348 CRC64;
     MTDNNTALKK AGLKVTLPRL KILEVLQEPD NHHVSAEDLY KRLIDMGEEI GLATVYRVLN
     QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSDDSIELR QREIASRHGI
     RLTNHSLYLY GHCAEGDCRE DEHAHDAVEK
//
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