NRPR1_METMA
ID NRPR1_METMA Reviewed; 323 AA.
AC Q8PXY1;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Global nitrogen regulator NrpRI {ECO:0000305};
DE AltName: Full=Nitrogen regulatory protein R I {ECO:0000305};
GN Name=nrpRI {ECO:0000303|PubMed:18415079};
GN OrderedLocusNames=MM_1085 {ECO:0000312|EMBL:AAM30781.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=18415079; DOI=10.1007/s00203-008-0369-3;
RA Weidenbach K., Ehlers C., Kock J., Ehrenreich A., Schmitz R.A.;
RT "Insights into the NrpR regulon in Methanosarcina mazei Goe1.";
RL Arch. Microbiol. 190:319-332(2008).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH NRPRII.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=20875081; DOI=10.1111/j.1742-4658.2010.07821.x;
RA Weidenbach K., Ehlers C., Kock J., Schmitz R.A.;
RT "NrpRII mediates contacts between NrpRI and general transcription factors
RT in the archaeon Methanosarcina mazei Goe1.";
RL FEBS J. 277:4398-4411(2010).
CC -!- FUNCTION: Plays a major role in nitrogen regulation. Under nitrogen
CC sufficiency, binds to the nifH and the glnk1 promoters, leading to
CC repression of the transcription of the genes.
CC {ECO:0000269|PubMed:18415079, ECO:0000269|PubMed:20875081}.
CC -!- ACTIVITY REGULATION: Under nitrogen limitation, binding of 2-
CC oxoglutarate to the NrpRI/NrpRII complex decreases the binding affinity
CC of NrpRI to DNA as well as the binding affinity of NrpRII to TBP and
CC TFB, which leads to removal of the complex from the operator, RNA
CC polymerase recruitment and initiation of transcription.
CC {ECO:0000269|PubMed:20875081}.
CC -!- SUBUNIT: Forms a complex with NrpRII and the general archaeal
CC transcription factors TBP and TFB. Interacts directly with NrpRII.
CC {ECO:0000269|PubMed:20875081}.
CC -!- INTERACTION:
CC Q8PXY1; Q8PVJ4: nrpRII; NbExp=3; IntAct=EBI-8377032, EBI-8377070;
CC -!- DISRUPTION PHENOTYPE: Disruption results in significantly increased
CC transcript levels of genes involved in nitrogen fixation or nitrogen
CC assimilation though growing under nitrogen sufficiency. It also leads
CC to a significant reduction of the lag-phase after a shift from nitrogen
CC sufficiency to nitrogen limitation. {ECO:0000269|PubMed:18415079}.
CC -!- SIMILARITY: Belongs to the NrpR family. {ECO:0000305}.
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; AE008384; AAM30781.1; -; Genomic_DNA.
DR RefSeq; WP_011033034.1; NC_003901.1.
DR AlphaFoldDB; Q8PXY1; -.
DR SMR; Q8PXY1; -.
DR IntAct; Q8PXY1; 1.
DR MINT; Q8PXY1; -.
DR STRING; 192952.MM_1085; -.
DR EnsemblBacteria; AAM30781; AAM30781; MM_1085.
DR GeneID; 44085662; -.
DR GeneID; 66137486; -.
DR KEGG; mma:MM_1085; -.
DR PATRIC; fig|192952.21.peg.1272; -.
DR eggNOG; arCOG02710; Archaea.
DR HOGENOM; CLU_073525_0_0_2; -.
DR OMA; IFIASRM; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.1360; -; 2.
DR InterPro; IPR002846; NRD.
DR InterPro; IPR038982; NrpR.
DR InterPro; IPR036984; NrpR_dom_sf.
DR InterPro; IPR013668; RNase_R_HTH_12.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR41964; PTHR41964; 1.
DR Pfam; PF08461; HTH_12; 1.
DR Pfam; PF01995; NRD1_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..323
FT /note="Global nitrogen regulator NrpRI"
FT /id="PRO_0000431495"
FT REGION 11..76
FT /note="Winged helix-turn-helix"
FT /evidence="ECO:0000305"
FT REGION 86..323
FT /note="NRD"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 35770 MW; 6060E3264D6EBA74 CRC64;
MMDPQIERKL IEIMRVIHES DKPIGARAIA DELNNRGYDI GERAVRYHLR ILDERGFTRK
HGYAGRTLTD LGENEMNDAL IGDRFGFVIS RIEEMAFRTT YNPETDKGDV VVNISYFDKD
DFETVIELIS YTAHAGYMIS PRVRIFEEDS LEMSLPPGKI GIATVCSVTF DGLLLKAGIP
VEPAYGGILQ IENKKPARFL DLISYSGTSI DPIKIFMNRT PTSVLEVLEK GEGKILANMR
QINSSAYEMT GKILKKAEKV GLAGCITLGE IDEYLLGAPV ETGKFGAAVV GGINGICALE
ETGIEIETNP ISTMLDYQTM KEI
