ID F9YAG1_KETVW Unreviewed; 142 AA.
AC F9YAG1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Ferric uptake regulation protein {ECO:0000256|ARBA:ARBA00020910, ECO:0000256|RuleBase:RU364037};
GN Name=fur {ECO:0000256|RuleBase:RU364037, ECO:0000313|EMBL:AEM41492.1};
GN OrderedLocusNames=KVU_1653 {ECO:0000313|EMBL:AEM41492.1};
OS Ketogulonicigenium vulgare (strain WSH-001).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=759362 {ECO:0000313|EMBL:AEM41492.1, ECO:0000313|Proteomes:UP000000692};
RN [1] {ECO:0000313|EMBL:AEM41492.1, ECO:0000313|Proteomes:UP000000692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSH-001 {ECO:0000313|EMBL:AEM41492.1,
RC ECO:0000313|Proteomes:UP000000692};
RX PubMed=21994934; DOI=10.1128/JB.06007-11;
RA Liu L., Li Y., Zhang J., Zhou Z., Liu J., Li X., Zhou J., Du G., Wang L.,
RA Chen J.;
RT "Complete genome sequence of the industrial strain Ketogulonicigenium
RT vulgare WSH-001.";
RL J. Bacteriol. 193:6108-6109(2011).
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 -!- 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}.
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DR EMBL; CP002018; AEM41492.1; -; Genomic_DNA.
DR RefSeq; WP_013384848.1; NC_017384.1.
DR RefSeq; YP_005795488.1; NC_017384.1.
DR AlphaFoldDB; F9YAG1; -.
DR KEGG; kvl:KVU_1653; -.
DR PATRIC; fig|759362.5.peg.1702; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_3_2_5; -.
DR OrthoDB; 8659436at2; -.
DR Proteomes; UP000000692; Chromosome.
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:PIRSR602481-2,
KW ECO:0000256|RuleBase:RU364037};
KW Reference proteome {ECO:0000313|Proteomes:UP000000692};
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|RuleBase:RU364037}.
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 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"
SQ SEQUENCE 142 AA; 16100 MW; 57C4DEE1C55729FB CRC64;
MAHSILGRCE AQGLRLTDQR RTIARILEGA DDHPDVAELH ARAVAVDSRI SIATVYRTVK
LLEEAGILER HEFGDGRARY EDADRDHHDH LIDMHSGEVV EFIDPEIEAL QEAIARKLGY
RLVGHRLELY GLRDSQSPEK KT
//
