FUR_PSEAE
ID FUR_PSEAE Reviewed; 134 AA.
AC Q03456;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=PA4764;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29260 / PA103;
RX PubMed=8478325; DOI=10.1128/jb.175.9.2589-2598.1993;
RA Prince R.W., Cox C.D., Vasil M.L.;
RT "Coordinate regulation of siderophore and exotoxin A production: molecular
RT cloning and sequencing of the Pseudomonas aeruginosa fur gene.";
RL J. Bacteriol. 175:2589-2598(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9852033; DOI=10.1128/jb.180.24.6784-6788.1998;
RA Vasil M.L., Ochsner U.A., Johnson Z., Colmer J.A., Hamood A.N.;
RT "The fur-regulated gene encoding the alternative sigma factor PvdS is
RT required for iron-dependent expression of the LysR-type regulator ptxR in
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 180:6784-6788(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, AND METAL-BINDING SITES.
RX PubMed=12581348; DOI=10.1046/j.1365-2958.2003.03337.x;
RA Pohl E., Haller J.C., Mijovilovich A., Meyer-Klaucke W., Garman E.,
RA Vasil M.L.;
RT "Architecture of a protein central to iron homeostasis: crystal structure
RT and spectroscopic analysis of the ferric uptake regulator.";
RL Mol. Microbiol. 47:903-915(2003).
CC -!- FUNCTION: Fur acts as a repressor, employing Fe(2+) as a cofactor to
CC bind the operator of the iron transport operon. Involved in exotoxin A
CC regulation, siderophore regulation and manganese susceptibility.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12581348}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; L00604; AAA25820.1; -; Genomic_DNA.
DR EMBL; AF050676; AAC05679.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08150.1; -; Genomic_DNA.
DR PIR; A40622; A40622.
DR RefSeq; NP_253452.1; NC_002516.2.
DR RefSeq; WP_003095216.1; NZ_QZGE01000018.1.
DR PDB; 1MZB; X-ray; 1.80 A; A=1-134.
DR PDB; 6H1C; X-ray; 2.34 A; A/B=1-134.
DR PDBsum; 1MZB; -.
DR PDBsum; 6H1C; -.
DR AlphaFoldDB; Q03456; -.
DR SMR; Q03456; -.
DR STRING; 287.DR97_2108; -.
DR World-2DPAGE; 0008:Q03456; -.
DR PaxDb; Q03456; -.
DR PRIDE; Q03456; -.
DR DNASU; 881780; -.
DR EnsemblBacteria; AAG08150; AAG08150; PA4764.
DR GeneID; 881780; -.
DR KEGG; pae:PA4764; -.
DR PATRIC; fig|208964.12.peg.4991; -.
DR PseudoCAP; PA4764; -.
DR HOGENOM; CLU_096072_3_3_6; -.
DR InParanoid; Q03456; -.
DR OMA; YLYGVCT; -.
DR PhylomeDB; Q03456; -.
DR BioCyc; PAER208964:G1FZ6-4877-MON; -.
DR EvolutionaryTrace; Q03456; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000c80; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0008198; F:ferrous iron binding; TAS:PseudoCAP.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051350; P:negative regulation of lyase activity; IMP:PseudoCAP.
DR GO; GO:1900705; P:negative regulation of siderophore biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:2000470; P:positive regulation of peroxidase activity; IMP:PseudoCAP.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:1901668; P:regulation of superoxide dismutase activity; IMP:PseudoCAP.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:CACAO.
DR CDD; cd07153; Fur_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.1490.190; -; 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; PTHR33202; 1.
DR Pfam; PF01475; FUR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Iron; Metal-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..134
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095567"
FT REGION 1..83
FT /note="DNA-binding"
FT REGION 84..134
FT /note="Dimerization"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:1MZB"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1MZB"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:6H1C"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1MZB"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1MZB"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1MZB"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1MZB"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1MZB"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1MZB"
SQ SEQUENCE 134 AA; 15234 MW; 99A35AD1E16677F2 CRC64;
MVENSELRKA GLKVTLPRVK ILQMLDSAEQ RHMSAEDVYK ALMEAGEDVG LATVYRVLTQ
FEAAGLVVRH NFDGGHAVFE LADSGHHDHM VCVDTGEVIE FMDAEIEKRQ KEIVRERGFE
LVDHNLVLYV RKKK
