ID B0SNF2_LEPBP Unreviewed; 140 AA.
AC B0SNF2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Putative ferric uptake regulation protein, Fur family (Ferric uptake regulator) {ECO:0000313|EMBL:ABZ98919.1};
GN OrderedLocusNames=LEPBI_I2849 {ECO:0000313|EMBL:ABZ98919.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ98919.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ98919.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000256|ARBA:ARBA00007957}.
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DR EMBL; CP000786; ABZ98919.1; -; Genomic_DNA.
DR RefSeq; WP_012389777.1; NC_010602.1.
DR AlphaFoldDB; B0SNF2; -.
DR STRING; 456481.LEPBI_I2849; -.
DR KEGG; lbi:LEPBI_I2849; -.
DR HOGENOM; CLU_096072_6_0_12; -.
DR OrthoDB; 8659436at2; -.
DR BioCyc; LBIF456481:LEPBI_RS13955-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
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: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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602481-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602481-1}.
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
SQ SEQUENCE 140 AA; 15807 MW; EBF6A3E509337A78 CRC64;
MAGDPSQILK KIGLKVTKNR EQVLSILQGS TRPLNHQEIM EKLPKEESWD RVTIYRALSD
LEEKNLLNSL HSADRVTYFE LKSDGNHIVS AAHGHLICNV CGKIECIDDP WNGMPSSKQL
KGFTTESVEI VFRGKCRNCQ
//