ID B2FHI8_STRMK Unreviewed; 163 AA.
AC B2FHI8;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Regulatory protein {ECO:0000313|EMBL:CAQ44981.1};
GN Name=fur {ECO:0000313|EMBL:CAQ44981.1};
GN OrderedLocusNames=Smlt1442 {ECO:0000313|EMBL:CAQ44981.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44981.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ44981.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ44981.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(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 -!- SIMILARITY: Belongs to the Fur family. {ECO:0000256|ARBA:ARBA00007957}.
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DR EMBL; AM743169; CAQ44981.1; -; Genomic_DNA.
DR RefSeq; WP_004150412.1; NC_010943.1.
DR AlphaFoldDB; B2FHI8; -.
DR EnsemblBacteria; CAQ44981; CAQ44981; Smlt1442.
DR GeneID; 84617007; -.
DR KEGG; sml:Smlt1442; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_2_1_6; -.
DR Proteomes; UP000008840; Chromosome.
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 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; ZINC UPTAKE REGULATION PROTEIN; 1.
DR PANTHER; PTHR33202:SF6; 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:UP000008840};
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 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
SQ SEQUENCE 163 AA; 17723 MW; 4DD4DD4447A30BCF CRC64;
MPAKTATACT APHHHVHDAS DFVAVVERVS RERGLRLTPI RANVLKLIAE AGKPVKAYEL
LEWVRNGKGV GADAPPTVYR ALDFLMANGF VHKLESVNAF VACHHPSSAA HSVPFLICNS
CHSAVELEDR EIVTQLEKRA KELGFQPQAQ TLEVHGLCAR CAG
//
