ID   NRDR_HERAR              Reviewed;         156 AA.
AC   A4G7M3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440};
GN   Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; OrderedLocusNames=HEAR2379;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- FUNCTION: Negatively regulates transcription of bacterial
CC       ribonucleotide reductase nrd genes and operons by binding to NrdR-
CC       boxes. {ECO:0000255|HAMAP-Rule:MF_00440}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00440};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00440};
CC   -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00440}.
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DR   EMBL; CU207211; CAL62510.1; -; Genomic_DNA.
DR   RefSeq; WP_011871773.1; NC_009138.1.
DR   AlphaFoldDB; A4G7M3; -.
DR   SMR; A4G7M3; -.
DR   STRING; 204773.HEAR2379; -.
DR   EnsemblBacteria; CAL62510; CAL62510; HEAR2379.
DR   KEGG; har:HEAR2379; -.
DR   eggNOG; COG1327; Bacteria.
DR   HOGENOM; CLU_108412_0_0_4; -.
DR   OMA; YRFTTYE; -.
DR   OrthoDB; 1551627at2; -.
DR   Proteomes; UP000006697; 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   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..156
FT                   /note="Transcriptional repressor NrdR"
FT                   /id="PRO_1000080758"
FT   DOMAIN          49..139
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00440"
FT   ZN_FING         3..34
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00440"
SQ   SEQUENCE   156 AA;  17928 MW;  DEF2D490039808C9 CRC64;
     MKCPFCQHDD TQVLDTRISE EGDSIRRRRR CVSCDKRFTT YERIELAMPV IVKKNGSRTD
     FDPKKLQASL QLALRKRPVS AEAVDAAIHR IEQKLLSSGE REVVSGQIGE LVMRELQRLD
     KIAYIRFASV YKSFEDVAEF QDAIAEVGRE RKPPSK