ISCR_ECOLI
ID ISCR_ECOLI Reviewed; 162 AA.
AC P0AGK8; P77484;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=HTH-type transcriptional regulator IscR;
GN Name=iscR; Synonyms=yfhP; OrderedLocusNames=b2531, JW2515;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND COFACTOR.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11742080; DOI=10.1073/pnas.251550898;
RA Schwartz C.J., Giel J.L., Patschkowski T., Luther C., Ruzicka F.J.,
RA Beinert H., Kiley P.J.;
RT "IscR, an Fe-S cluster-containing transcription factor, represses
RT expression of Escherichia coli genes encoding Fe-S cluster assembly
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14895-14900(2001).
RN [5]
RP REGULATION OF BIOGENESIS OF FE-S-CONTAINING CLUSTERS AND PROTEINS, AND
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16677314; DOI=10.1111/j.1365-2958.2006.05160.x;
RA Giel J.L., Rodionov D., Liu M., Blattner F.R., Kiley P.J.;
RT "IscR-dependent gene expression links iron-sulphur cluster assembly to the
RT control of O2-regulated genes in Escherichia coli.";
RL Mol. Microbiol. 60:1058-1075(2006).
RN [6]
RP FUNCTION IN ACTIVATION OF SUF OPERON, AND MUTAGENESIS OF CYS-92; CYS-98 AND
RP CYS-104.
RC STRAIN=K12 / GC4468;
RX PubMed=16824106; DOI=10.1111/j.1365-2958.2006.05220.x;
RA Yeo W.-S., Lee J.-H., Lee K.-C., Roe J.-H.;
RT "IscR acts as an activator in response to oxidative stress for the suf
RT operon encoding Fe-S assembly proteins.";
RL Mol. Microbiol. 61:206-218(2006).
RN [7]
RP FUNCTION IN REPRESSION OF RNLA, DNA-BINDING, AND MUTAGENESIS OF CYS-92;
RP CYS-98 AND CYS-104.
RC STRAIN=K12;
RX PubMed=20421606; DOI=10.1534/genetics.110.114462;
RA Otsuka Y., Miki K., Koga M., Katayama N., Morimoto W., Takahashi Y.,
RA Yonesaki T.;
RT "IscR regulates RNase LS activity by repressing rnlA transcription.";
RL Genetics 185:823-830(2010).
CC -!- FUNCTION: Regulates the transcription of several operons and genes
CC involved in the biogenesis of Fe-S clusters and Fe-S-containing
CC proteins. Transcriptional repressor of the iscRSUA operon, which is
CC involved in the assembly of Fe-S clusters into Fe-S proteins. In its
CC apoform, under conditions of oxidative stress or iron deprivation, it
CC activates the suf operon, which is a second operon involved in the
CC assembly of Fe-S clusters. Represses its own transcription as well as
CC that of toxin rnlA. {ECO:0000269|PubMed:11742080,
CC ECO:0000269|PubMed:16824106, ECO:0000269|PubMed:20421606}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:11742080, ECO:0000269|PubMed:16677314};
CC Note=Binds 1 [2Fe-2S] cluster; whether or not the Fe-S cluster is
CC necessary for transcriptional regulation depends on the type of IscR-
CC binding sequence. {ECO:0000269|PubMed:11742080,
CC ECO:0000269|PubMed:16677314};
CC -!- INTERACTION:
CC P0AGK8; P0AGK8: iscR; NbExp=2; IntAct=EBI-1129278, EBI-1129278;
CC -!- INDUCTION: By oxidative stress conditions and iron starvation.
CC {ECO:0000269|PubMed:16677314}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75584.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16425.1; -; Genomic_DNA.
DR PIR; B65030; B65030.
DR RefSeq; NP_417026.1; NC_000913.3.
DR RefSeq; WP_001241357.1; NZ_STEB01000011.1.
DR PDB; 4HF0; X-ray; 1.90 A; A/B=1-133.
DR PDB; 4HF1; X-ray; 2.22 A; A/B=1-162.
DR PDB; 4HF2; X-ray; 2.99 A; A/B=1-162.
DR PDBsum; 4HF0; -.
DR PDBsum; 4HF1; -.
DR PDBsum; 4HF2; -.
DR AlphaFoldDB; P0AGK8; -.
DR SMR; P0AGK8; -.
DR BioGRID; 4259433; 82.
DR BioGRID; 849657; 1.
DR DIP; DIP-47974N; -.
DR IntAct; P0AGK8; 4.
DR STRING; 511145.b2531; -.
DR jPOST; P0AGK8; -.
DR PaxDb; P0AGK8; -.
DR PRIDE; P0AGK8; -.
DR EnsemblBacteria; AAC75584; AAC75584; b2531.
DR EnsemblBacteria; BAA16425; BAA16425; BAA16425.
DR GeneID; 60903810; -.
DR GeneID; 945279; -.
DR KEGG; ecj:JW2515; -.
DR KEGG; eco:b2531; -.
DR PATRIC; fig|1411691.4.peg.4203; -.
DR EchoBASE; EB3178; -.
DR eggNOG; COG1959; Bacteria.
DR HOGENOM; CLU_107144_0_0_6; -.
DR InParanoid; P0AGK8; -.
DR OMA; YGLTIMM; -.
DR PhylomeDB; P0AGK8; -.
DR BioCyc; EcoCyc:G7326-MON; -.
DR PRO; PR:P0AGK8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_01176; HTH_type_IscR; 1.
DR InterPro; IPR010242; TF_HTH_IscR.
DR InterPro; IPR030489; TR_Rrf2-type_CS.
DR InterPro; IPR000944; Tscrpt_reg_Rrf2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33221; PTHR33221; 1.
DR Pfam; PF02082; Rrf2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR02010; IscR; 1.
DR TIGRFAMs; TIGR00738; rrf2_super; 1.
DR PROSITE; PS01332; HTH_RRF2_1; 1.
DR PROSITE; PS51197; HTH_RRF2_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Activator; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repressor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..162
FT /note="HTH-type transcriptional regulator IscR"
FT /id="PRO_0000109560"
FT DOMAIN 2..131
FT /note="HTH rrf2-type"
FT DNA_BIND 28..51
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT MUTAGEN 92
FT /note="C->A: No effect on activation of the suf operon, no
FT effect on repression of rnlA."
FT /evidence="ECO:0000269|PubMed:16824106,
FT ECO:0000269|PubMed:20421606"
FT MUTAGEN 98
FT /note="C->A: No effect on activation of the suf operon, no
FT effect on repression of rnlA."
FT /evidence="ECO:0000269|PubMed:16824106,
FT ECO:0000269|PubMed:20421606"
FT MUTAGEN 104
FT /note="C->A: No effect on activation of the suf operon, no
FT effect on repression of rnlA."
FT /evidence="ECO:0000269|PubMed:16824106,
FT ECO:0000269|PubMed:20421606"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:4HF0"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4HF0"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4HF2"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4HF1"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:4HF0"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:4HF0"
SQ SEQUENCE 162 AA; 17337 MW; DE82977C3774E3BD CRC64;
MRLTSKGRYA VTAMLDVALN SEAGPVPLAD ISERQGISLS YLEQLFSRLR KNGLVSSVRG
PGGGYLLGKD ASSIAVGEVI SAVDESVDAT RCQGKGGCQG GDKCLTHALW RDLSDRLTGF
LNNITLGELV NNQEVLDVSG RQHTHDAPRT RTQDAIDVKL RA
