FURA_MYCTU
ID FURA_MYCTU Reviewed; 147 AA.
AC P9WN87; L0T9L6; O07715; O07724; P0A582;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Transcriptional regulator FurA;
GN Name=furA; Synonyms=fur; OrderedLocusNames=Rv1909c; ORFNames=MTCY180.09;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RA Song J., Deretic V.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11401695; DOI=10.1046/j.1365-2958.2001.02427.x;
RA Pym A.S., Domenech P., Honore N., Song J., Deretic V., Cole S.T.;
RT "Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity
RT and virulence by furA of Mycobacterium tuberculosis.";
RL Mol. Microbiol. 40:879-889(2001).
RN [4]
RP FUNCTION, DNA-BINDING, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12949087; DOI=10.1128/jb.185.18.5357-5362.2003;
RA Sala C., Forti F., Di Florio E., Canneva F., Milano A., Riccardi G.,
RA Ghisotti D.;
RT "Mycobacterium tuberculosis FurA autoregulates its own expression.";
RL J. Bacteriol. 185:5357-5362(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Represses transcription of the catalase-peroxidase gene katG
CC and its own transcription by binding to the promoter region in a redox-
CC dependent manner. {ECO:0000269|PubMed:11401695,
CC ECO:0000269|PubMed:12949087}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:11401695,
CC ECO:0000269|PubMed:12949087}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; AF002194; AAB63370.1; -; Genomic_DNA.
DR EMBL; AF012630; AAB66826.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44676.1; -; Genomic_DNA.
DR PIR; B70519; B70519.
DR RefSeq; NP_216425.2; NC_000962.3.
DR RefSeq; WP_003899076.1; NZ_NVQJ01000034.1.
DR AlphaFoldDB; P9WN87; -.
DR SMR; P9WN87; -.
DR STRING; 83332.Rv1909c; -.
DR PaxDb; P9WN87; -.
DR DNASU; 885400; -.
DR GeneID; 45425880; -.
DR GeneID; 885400; -.
DR KEGG; mtu:Rv1909c; -.
DR TubercuList; Rv1909c; -.
DR eggNOG; COG0735; Bacteria.
DR OMA; DHPHADT; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MTBBASE.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MTBBASE.
DR GO; GO:0010039; P:response to iron ion; IEP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
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 Cytoplasm; DNA-binding; Iron; Metal-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..147
FT /note="Transcriptional regulator FurA"
FT /id="PRO_0000095562"
FT REGION 1..85
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 86..147
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 82
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 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 147 AA; 15892 MW; 10A669FA89CB5281 CRC64;
MSSIPDYAEQ LRTADLRVTR PRVAVLEAVN AHPHADTETI FGAVRFALPD VSRQAVYDVL
HALTAAGLVR KIQPSGSVAR YESRVGDNHH HIVCRSCGVI ADVDCAVGEA PCLTASDHNG
FLLDEAEVIY WGLCPDCSIS DTSRSHP
