IDER_MYCTU
ID IDER_MYCTU Reviewed; 230 AA.
AC P9WMH1; L0TC16; O08190; P0A672; Q50495;
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=Iron-dependent repressor IdeR;
GN Name=ideR; Synonyms=dtxR; OrderedLocusNames=Rv2711; ORFNames=MTCY05A6.32;
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;
RX PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8;
RA Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., Cole S.T.,
RA Smith D.R., Smith I.;
RT "Genomic organization of the mycobacterial sigma gene cluster.";
RL Gene 165:67-70(1995).
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 DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11722747; DOI=10.1046/j.1365-2958.2001.02684.x;
RA Gold B., Rodriguez G.M., Marras S.A.E., Pentecost M., Smith I.;
RT "The Mycobacterium tuberculosis IdeR is a dual functional regulator that
RT controls transcription of genes involved in iron acquisition, iron storage
RT and survival in macrophages.";
RL Mol. Microbiol. 42:851-865(2001).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-140, AND SUBUNIT.
RX PubMed=9887269; DOI=10.1006/jmbi.1998.2339;
RA Pohl E., Holmes R.K., Hol W.G.J.;
RT "Crystal structure of the iron-dependent regulator (IdeR) from
RT Mycobacterium tuberculosis shows both metal binding sites fully occupied.";
RL J. Mol. Biol. 285:1145-1156(1999).
CC -!- FUNCTION: Metal-dependent DNA-binding protein that controls
CC transcription of many genes involved in iron metabolism. Acts as a
CC repressor of siderophore biosynthesis and as a positive modulator of
CC iron storage. Also regulates expression of transporters, proteins
CC involved in siderophore synthesis, iron storage and transcriptional
CC regulators. {ECO:0000269|PubMed:11722747, ECO:0000269|PubMed:12065475}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9887269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the DtxR/MntR family. {ECO:0000305}.
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DR EMBL; U14191; AAA86057.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45509.1; -; Genomic_DNA.
DR PIR; B70532; B70532.
DR RefSeq; NP_217227.1; NC_000962.3.
DR RefSeq; WP_003413962.1; NZ_NVQJ01000017.1.
DR PDB; 1B1B; X-ray; 2.60 A; A=1-140.
DR PDB; 1FX7; X-ray; 2.00 A; A/B/C/D=1-230.
DR PDB; 1U8R; X-ray; 2.75 A; A/B/C/D/G/H/I/J=1-230.
DR PDB; 2ISY; X-ray; 1.96 A; A/B=1-140.
DR PDB; 2ISZ; X-ray; 2.40 A; A/B/C/D=1-140.
DR PDB; 2IT0; X-ray; 2.60 A; A/B/C/D=1-140.
DR PDBsum; 1B1B; -.
DR PDBsum; 1FX7; -.
DR PDBsum; 1U8R; -.
DR PDBsum; 2ISY; -.
DR PDBsum; 2ISZ; -.
DR PDBsum; 2IT0; -.
DR AlphaFoldDB; P9WMH1; -.
DR SMR; P9WMH1; -.
DR STRING; 83332.Rv2711; -.
DR PaxDb; P9WMH1; -.
DR DNASU; 888590; -.
DR GeneID; 45426698; -.
DR GeneID; 888590; -.
DR KEGG; mtu:Rv2711; -.
DR TubercuList; Rv2711; -.
DR eggNOG; COG1321; Bacteria.
DR OMA; DAQLMYT; -.
DR PhylomeDB; P9WMH1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0046870; F:cadmium ion binding; IDA:MTBBASE.
DR GO; GO:0050897; F:cobalt ion binding; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008198; F:ferrous iron binding; IDA:MTBBASE.
DR GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0016151; F:nickel cation binding; IDA:MTBBASE.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; IMP:MTBBASE.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.60.10; -; 1.
DR Gene3D; 2.30.30.90; -; 1.
DR InterPro; IPR040767; DtxR_SH3.
DR InterPro; IPR007167; Fe-transptr_FeoA.
DR InterPro; IPR001367; Fe_dep_repressor.
DR InterPro; IPR036421; Fe_dep_repressor_sf.
DR InterPro; IPR038157; FeoA_core_dom.
DR InterPro; IPR022687; HTH_DTXR.
DR InterPro; IPR022689; Iron_dep_repressor.
DR InterPro; IPR008988; Transcriptional_repressor_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF18357; DtxR; 1.
DR Pfam; PF02742; Fe_dep_repr_C; 1.
DR Pfam; PF01325; Fe_dep_repress; 1.
DR SMART; SM00899; FeoA; 1.
DR SMART; SM00529; HTH_DTXR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47979; SSF47979; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR PROSITE; PS50944; HTH_DTXR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Iron; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..230
FT /note="Iron-dependent repressor IdeR"
FT /id="PRO_0000201108"
FT DOMAIN 4..65
FT /note="HTH dtxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00296"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1U8R"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2ISY"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2ISY"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 66..88
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2ISY"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2ISY"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:1FX7"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1FX7"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1U8R"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1FX7"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1FX7"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1FX7"
SQ SEQUENCE 230 AA; 25233 MW; 77B9CA98E04BDC27 CRC64;
MNELVDTTEM YLRTIYDLEE EGVTPLRARI AERLDQSGPT VSQTVSRMER DGLLRVAGDR
HLELTEKGRA LAIAVMRKHR LAERLLVDVI GLPWEEVHAE ACRWEHVMSE DVERRLVKVL
NNPTTSPFGN PIPGLVELGV GPEPGADDAN LVRLTELPAG SPVAVVVRQL TEHVQGDIDL
ITRLKDAGVV PNARVTVETT PGGGVTIVIP GHENVTLPHE MAHAVKVEKV
