NRPR_METMP
ID NRPR_METMP Reviewed; 536 AA.
AC Q6LZL7; Q8J2Z0;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Global nitrogen regulator NrpR {ECO:0000305};
DE AltName: Full=Nitrogen regulatory protein R {ECO:0000303|PubMed:12492867};
GN Name=nrpR {ECO:0000303|PubMed:12492867};
GN OrderedLocusNames=MMP0607 {ECO:0000312|EMBL:CAF30163.1};
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
RP DNA-BINDING, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=S2 / LL;
RX PubMed=12492867; DOI=10.1046/j.1365-2958.2003.03293.x;
RA Lie T.J., Leigh J.A.;
RT "A novel repressor of nif and glnA expression in the methanogenic archaeon
RT Methanococcus maripaludis.";
RL Mol. Microbiol. 47:235-246(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [3]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=S2 / LL;
RX PubMed=15590692; DOI=10.1074/jbc.m411778200;
RA Lie T.J., Wood G.E., Leigh J.A.;
RT "Regulation of nif expression in Methanococcus maripaludis: roles of the
RT euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators.";
RL J. Biol. Chem. 280:5236-5241(2005).
RN [4]
RP MUTAGENESIS OF CYS-148; LEU-195; CYS-389 AND HIS-435.
RX PubMed=17720835; DOI=10.1128/aem.01324-07;
RA Lie T.J., Leigh J.A.;
RT "Genetic screen for regulatory mutations in Methanococcus maripaludis and
RT its use in identification of induction-deficient mutants of the
RT euryarchaeal repressor NrpR.";
RL Appl. Environ. Microbiol. 73:6595-6600(2007).
CC -!- FUNCTION: Transcriptional repressor of nitrogen fixation and
CC assimilation genes. Binds to two tandem operators in the glnA and nif
CC promoters, thereby blocking transcription of the genes.
CC {ECO:0000269|PubMed:12492867, ECO:0000269|PubMed:15590692}.
CC -!- ACTIVITY REGULATION: Under nitrogen limitation, binding of the
CC intracellular nitrogen metabolite 2-oxoglutarate to NrpR decreases the
CC binding affinity of NrpR to DNA, leading to initiation of
CC transcription. {ECO:0000269|PubMed:15590692}.
CC -!- SUBUNIT: Homotetramer. Binds to a single operator as a dimer and
CC cooperatively to two operators as a dimer pair.
CC {ECO:0000269|PubMed:12492867, ECO:0000269|PubMed:15590692}.
CC -!- INTERACTION:
CC Q6LZL7; Q6LZL7: nrpR; NbExp=2; IntAct=EBI-15891928, EBI-15891928;
CC -!- DISRUPTION PHENOTYPE: Disruption results in slower growth with ammonia,
CC but does not affect growth under nitrogen-fixing conditions.
CC {ECO:0000269|PubMed:12492867}.
CC -!- SIMILARITY: Belongs to the NrpR family. {ECO:0000305}.
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DR EMBL; AY157992; AAN77506.1; -; Genomic_DNA.
DR EMBL; BX950229; CAF30163.1; -; Genomic_DNA.
DR RefSeq; WP_011170551.1; NC_005791.1.
DR AlphaFoldDB; Q6LZL7; -.
DR SMR; Q6LZL7; -.
DR DIP; DIP-59017N; -.
DR STRING; 267377.MMP0607; -.
DR PRIDE; Q6LZL7; -.
DR DNASU; 2761666; -.
DR EnsemblBacteria; CAF30163; CAF30163; MMP0607.
DR GeneID; 2761666; -.
DR KEGG; mmp:MMP0607; -.
DR PATRIC; fig|267377.15.peg.621; -.
DR eggNOG; arCOG02710; Archaea.
DR HOGENOM; CLU_507744_0_0_2; -.
DR OMA; FEDYEPV; -.
DR OrthoDB; 7749at2157; -.
DR BioCyc; MMAR267377:MMP_RS03195-MON; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.1360; -; 3.
DR InterPro; IPR002846; NRD.
DR InterPro; IPR038982; NrpR.
DR InterPro; IPR036984; NrpR_dom_sf.
DR InterPro; IPR013668; RNase_R_HTH_12.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR41964; PTHR41964; 2.
DR Pfam; PF08461; HTH_12; 1.
DR Pfam; PF01995; NRD1_2; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..536
FT /note="Global nitrogen regulator NrpR"
FT /id="PRO_0000431494"
FT REGION 7..72
FT /note="Winged helix-turn-helix"
FT /evidence="ECO:0000250|UniProtKB:Q57623"
FT REGION 80..314
FT /note="NRD 1"
FT /evidence="ECO:0000250|UniProtKB:Q57623"
FT REGION 315..536
FT /note="NRD 2"
FT /evidence="ECO:0000250|UniProtKB:Q57623"
FT MUTAGEN 148
FT /note="C->A: Decreases response to 2-oxoglutarate."
FT /evidence="ECO:0000269|PubMed:17720835"
FT MUTAGEN 195
FT /note="L->A: Decreases response to 2-oxoglutarate."
FT /evidence="ECO:0000269|PubMed:17720835"
FT MUTAGEN 389
FT /note="C->A: Decreases response to 2-oxoglutarate."
FT /evidence="ECO:0000269|PubMed:17720835"
FT MUTAGEN 435
FT /note="H->A: Decreases response to 2-oxoglutarate."
FT /evidence="ECO:0000269|PubMed:17720835"
FT CONFLICT 14
FT /note="S -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305|PubMed:12492867"
SQ SEQUENCE 536 AA; 59602 MW; FA34D88914B75D9E CRC64;
MDSNIDVEIL SILSEASAPV GAKIIADSLK DRGYDIGERA VRYHLKVLDE NSLTKKLGYS
GREITEKGIE ELEKANISFR IGSVFSQVIE KLYLSDFPSK VLINTAKFEG DYKTIKEMVL
RSFEAGYSVG DYLNIKKKGN TVSVETLCSI TFDNFLLKNG IIPTPEYGGI VKFEDYEPVN
FEGVIDFKSS SIDPLVAFIM QGKTDVIGVI ENGEGLVPAN FRVIPKSSEK QFETILKKDM
LNSVLAYGTE NVLGMNLNPE QIGVVLVGGL TPLCVPHESG YTADISAATQ LKDISSMEKK
TKGFLEAKKK KGKFKVTPVL SKMLSKMQTI NYDIEDKKGN VVVNTAKIPI EYKEEAINAL
KDSYENKLAI SDRLKVECDD KFLNAYTICS LTVDGVFLKN KIPVIPYYGG ILEVKADKKR
FIEAIDYEGT SLDPHEVFFN KADGKNYILA GIRKVPMSAS EKLIELNEKL GWNSIIEIGR
PNNDICGVRV EKCMFGITTI GGTNPFANIR KNNIPVEMKT LHKSIDYSEL THYDDI
