ID   NRDR_BORPD              Reviewed;         158 AA.
AC   A9I295;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440};
GN   Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; OrderedLocusNames=Bpet0615;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP40947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I295; -.
DR   SMR; A9I295; -.
DR   STRING; 94624.Bpet0615; -.
DR   EnsemblBacteria; CAP40947; CAP40947; Bpet0615.
DR   KEGG; bpt:Bpet0615; -.
DR   eggNOG; COG1327; Bacteria.
DR   OMA; YRFTTYE; -.
DR   Proteomes; UP000001225; 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..158
FT                   /note="Transcriptional repressor NrdR"
FT                   /id="PRO_1000124471"
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   158 AA;  17940 MW;  5CA8AC5ACDDEDC4B CRC64;
     MKCPFCGNAD TQVVDSRVSE EGDTIRRRRR CLSCDKRFTT YERIELAMPS VVKRNGSRSD
     YDTAKLRASL SLALRKRPVS TDQVDSVVAR IEETLLASGQ REVSTERIGE LVMAELKKLD
     KVGYVRFASV YKNFEDIGEF VDAIREMQGP MLPGKLRK