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NRDR_STRCO
ID   NRDR_STRCO              Reviewed;         182 AA.
AC   O69980; Q4QZ21;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Transcriptional repressor NrdR;
GN   Name=nrdR; OrderedLocusNames=SCO5804; ORFNames=SC4H2.25;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Borovok I.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=15522084; DOI=10.1111/j.1365-2958.2004.04325.x;
RA   Borovok I., Gorovitz B., Yanku M., Schreiber R., Gust B., Chater K.,
RA   Aharonowitz Y., Cohen G.;
RT   "Alternative oxygen-dependent and oxygen-independent ribonucleotide
RT   reductases in Streptomyces: cross-regulation and physiological role in
RT   response to oxygen limitation.";
RL   Mol. Microbiol. 54:1022-1035(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=15949864; DOI=10.1016/j.tig.2005.05.011;
RA   Rodionov D.A., Gelfand M.S.;
RT   "Identification of a bacterial regulatory system for ribonucleotide
RT   reductases by phylogenetic profiling.";
RL   Trends Genet. 21:385-389(2005).
RN   [5]
RP   FUNCTION, ZINC-FINGER, COFACTOR, PROTEIN REGULATION, AND MUTAGENESIS OF
RP   CYS-3 AND 50-LYS-ARG-51.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=16950922; DOI=10.1128/jb.00903-06;
RA   Grinberg I., Shteinberg T., Gorovitz B., Aharonowitz Y., Cohen G.,
RA   Borovok I.;
RT   "The Streptomyces NrdR transcriptional regulator is a Zn ribbon/ATP cone
RT   protein that binds to the promoter regions of class Ia and class II
RT   ribonucleotide reductase operons.";
RL   J. Bacteriol. 188:7635-7644(2006).
CC   -!- FUNCTION: Negatively regulates transcription of nrdRJ (class II RNR
CC       genes) and nrdABS operon (class I RNR genes) by binding to NrdR-boxes
CC       which are proximal to or overlap with the promoter regions of class II
CC       and class Ia RNR operons, respectively. {ECO:0000269|PubMed:15522084,
CC       ECO:0000269|PubMed:15949864, ECO:0000269|PubMed:16950922}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16950922};
CC       Note=Binds 1 zinc ion. {ECO:0000269|PubMed:16950922};
CC   -!- DOMAIN: The ATP-cone domain may function to recruit ATP/dATP to elicit
CC       a conformational change in NrdR that is necessary for binding.
CC   -!- DISRUPTION PHENOTYPE: Cells up-regulate expression of nrdRJ and nrdABS
CC       transcription. A mutant in which amino acids 1 to 41 are deleted is
CC       unable to bind zinc and also unable to bind the nrdABS and nrdRJ
CC       promoters. A mutant in which amino acids 151 to 182 are deleted is able
CC       to bind to both promoters to the same extent as the wild-type.
CC       Functional zinc-finger and ATP-cone domain are required for binding to
CC       the promoter regions of both sets of RNR genes.
CC       {ECO:0000269|PubMed:15522084}.
CC   -!- MISCELLANEOUS: Seems to be allosterically activated by ATP/dATP.
CC   -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000305}.
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DR   EMBL; AM039891; CAJ01781.1; -; Genomic_RNA.
DR   EMBL; AL939125; CAA18340.1; -; Genomic_DNA.
DR   PIR; T35124; T35124.
DR   RefSeq; NP_629928.1; NC_003888.3.
DR   RefSeq; WP_003973218.1; NZ_VNID01000007.1.
DR   AlphaFoldDB; O69980; -.
DR   SMR; O69980; -.
DR   STRING; 100226.SCO5804; -.
DR   GeneID; 1101246; -.
DR   KEGG; sco:SCO5804; -.
DR   PATRIC; fig|100226.15.peg.5896; -.
DR   eggNOG; COG1327; Bacteria.
DR   HOGENOM; CLU_108412_1_0_11; -.
DR   InParanoid; O69980; -.
DR   OMA; YRFTTYE; -.
DR   PhylomeDB; O69980; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00440; NrdR; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR003796; RNR_NrdR-like.
DR   PANTHER; PTHR30455; PTHR30455; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   TIGRFAMs; TIGR00244; TIGR00244; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..182
FT                   /note="Transcriptional repressor NrdR"
FT                   /id="PRO_0000182365"
FT   DOMAIN          46..136
FT                   /note="ATP-cone"
FT   ZN_FING         3..34
FT   REGION          144..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         3
FT                   /note="C->A: 7-fold reduction in the amount of zinc bound.
FT                   No binding to nrdABS and nrdRJ promoters."
FT                   /evidence="ECO:0000269|PubMed:16950922"
FT   MUTAGEN         50..51
FT                   /note="KR->NG: Loss of ATP/dATP binding. Weak binding to
FT                   nrdABS and nrdRJ promoters."
FT                   /evidence="ECO:0000269|PubMed:16950922"
SQ   SEQUENCE   182 AA;  19719 MW;  4AC39D1114B9567A CRC64;
     MHCPFCRHPD SRVVDSRTTD DGTSIRRRRQ CPDCSRRFTT VETCSLMVVK RSGVTEPFSR
     TKVINGVRKA CQGRPVTEDA LAQLGQRVEE AVRATGSAEL TTHDVGLAIL GPLQELDLVA
     YLRFASVYRA FDSLEDFEAA IAELRETTGH PGEEDDTGAG SQENDRGPTG AGQVPEPAGA
     AD
 
 
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