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FUR_YERPE
ID   FUR_YERPE               Reviewed;         148 AA.
AC   P33086; Q0WDQ0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Ferric uptake regulation protein;
DE            Short=Ferric uptake regulator;
GN   Name=fur; OrderedLocusNames=YPO2634, y1208, YP_1081;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM6;
RX   PubMed=1406286; DOI=10.1111/j.1365-2958.1992.tb01427.x;
RA   Staggs T.M., Perry R.D.;
RT   "Fur regulation in Yersinia species.";
RL   Mol. Microbiol. 6:2507-2516(1992).
RN   [2]
RP   SEQUENCE REVISION TO 57-61.
RX   PubMed=8559079;
RA   Staggs T.M., Perry R.D.;
RT   "Fur regulation in Yersinia species.";
RL   Mol. Microbiol. 17:601-601(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM6;
RA   Bearden S.W.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Fur acts as a repressor, employing Fe(2+) as a cofactor to
CC       bind the operator of the iron transport operon.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR   EMBL; Z12101; CAA78082.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL21256.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM84784.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS61329.1; -; Genomic_DNA.
DR   PIR; AE0321; AE0321.
DR   PIR; S70733; S70733.
DR   RefSeq; WP_002210357.1; NZ_WUCM01000102.1.
DR   RefSeq; YP_002347588.1; NC_003143.1.
DR   AlphaFoldDB; P33086; -.
DR   SMR; P33086; -.
DR   STRING; 214092.YPO2634; -.
DR   PaxDb; P33086; -.
DR   DNASU; 1146155; -.
DR   EnsemblBacteria; AAM84784; AAM84784; y1208.
DR   EnsemblBacteria; AAS61329; AAS61329; YP_1081.
DR   GeneID; 57976058; -.
DR   KEGG; ype:YPO2634; -.
DR   KEGG; ypk:y1208; -.
DR   KEGG; ypm:YP_1081; -.
DR   PATRIC; fig|214092.21.peg.3066; -.
DR   eggNOG; COG0735; Bacteria.
DR   HOGENOM; CLU_096072_3_3_6; -.
DR   OMA; MKHFAIF; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   CollecTF; EXPREG_00000a20; -.
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:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:1900705; P:negative regulation of siderophore biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; EXP:CollecTF.
DR   GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Iron; Metal-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..148
FT                   /note="Ferric uptake regulation protein"
FT                   /id="PRO_0000095588"
FT   REGION          1..84
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          85..142
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        21
FT                   /note="K -> T (in Ref. 6; AAS61329)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58..60
FT                   /note="VLN -> CSE (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   148 AA;  16728 MW;  4084639E45ACFDB7 CRC64;
     MTDNNKALKN AGLKVTLPRL KILEVLQNPA CHHVSAEDLY KILIDIGEEI GLATVYRVLN
     QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSNESIESL QREIAKQHGI
     KLTNHSLYLY GHCETGNCRE DESAHSKR
 
 
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