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Database: UniProt
Entry: Q7AUU7_9GAMM
LinkDB: Q7AUU7_9GAMM
Original site: Q7AUU7_9GAMM 
ID   Q7AUU7_9GAMM            Unreviewed;       147 AA.
AC   Q7AUU7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:CAD26839.1};
OS   Aliivibrio salmonicida.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=40269 {ECO:0000313|EMBL:CAD26839.1};
RN   [1] {ECO:0000313|EMBL:CAD26839.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NVI 87/09/1193 {ECO:0000313|EMBL:CAD26839.1};
RX   PubMed=12383519; DOI=10.1016/S0378-1119(02)00863-6;
RA   Colquhoun D.J., Sorum H.;
RT   "Cloning, characterisation and phylogenetic analysis of the fur gene in
RT   Vibrio salmonicida and Vibrio logei.";
RL   Gene 296:213-220(2002).
RN   [2] {ECO:0000313|EMBL:CAD26839.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NVI 87/09/1193 {ECO:0000313|EMBL:CAD26839.1};
RA   Colquhoun D.J.;
RT   "Vibrio salmonicida the causative agent of cold water vibriosis: factors of
RT   importance for pathogenesis and vaccine protection.";
RL   Thesis (2002), Department of Dept. Pharm., Microbiol., and Food Hyg.,
RL   Norwegian School of Veterinary Science, Oslo, Norway.
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}.
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DR   EMBL; AJ437614; CAD26839.1; -; Genomic_DNA.
DR   RefSeq; WP_012549620.1; NZ_CP034240.1.
DR   AlphaFoldDB; Q7AUU7; -.
DR   OMA; YLYGVCT; -.
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   147 AA;  16636 MW;  BEC5780B95950333 CRC64;
     MSDNNQALKK AGLKVTLPRL KILEILQQPE SQHISAEDLY KKLIDIGEEI GLATVYRVLN
     QFDDAGIVTR HHFEGGKSVF ELATQHHHDH LVCLDCGKVI EFSDDLIEER QKDIANKYNV
     RLTNHSLYLY GHCITGDCIE NTTAHNG
//
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