NRPR_METJA
ID NRPR_METJA Reviewed; 542 AA.
AC Q57623;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Global nitrogen regulator NrpR {ECO:0000305};
DE AltName: Full=Nitrogen regulatory protein R {ECO:0000305};
GN Name=nrpR {ECO:0000303|PubMed:21070950};
GN OrderedLocusNames=MJ0159 {ECO:0000312|EMBL:AAB98143.1};
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 306-542, DNA-BINDING, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=21070950; DOI=10.1016/j.str.2010.08.014;
RA Wisedchaisri G., Dranow D.M., Lie T.J., Bonanno J.B., Patskovsky Y.,
RA Ozyurt S.A., Sauder J.M., Almo S.C., Wasserman S.R., Burley S.K.,
RA Leigh J.A., Gonen T.;
RT "Structural underpinnings of nitrogen regulation by the prototypical
RT nitrogen-responsive transcriptional factor NrpR.";
RL Structure 18:1512-1521(2010).
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:0000250|UniProtKB:Q6LZL7}.
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:21070950}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21070950}.
CC -!- MISCELLANEOUS: Adopts different quaternary structures in its active apo
CC state compared with its inhibited 2-oxoglutarate-bound state. In the 2-
CC oxoglutarate-bound state, NrpR is inhibited from binding to DNA because
CC its DNA-binding domains are too far apart to recognize the operator DNA
CC sequence. {ECO:0000269|PubMed:21070950}.
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; L77117; AAB98143.1; -; Genomic_DNA.
DR PIR; H64319; H64319.
DR PDB; 3NEK; X-ray; 2.50 A; A/B=306-542.
DR PDBsum; 3NEK; -.
DR AlphaFoldDB; Q57623; -.
DR SMR; Q57623; -.
DR DIP; DIP-59016N; -.
DR STRING; 243232.MJ_0159; -.
DR DNASU; 1451006; -.
DR EnsemblBacteria; AAB98143; AAB98143; MJ_0159.
DR KEGG; mja:MJ_0159; -.
DR eggNOG; arCOG02710; Archaea.
DR HOGENOM; CLU_507744_0_0_2; -.
DR InParanoid; Q57623; -.
DR OMA; FEDYEPV; -.
DR PhylomeDB; Q57623; -.
DR EvolutionaryTrace; Q57623; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.1360; -; 4.
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; 2.
DR Pfam; PF08461; HTH_12; 1.
DR Pfam; PF01995; NRD1_2; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..542
FT /note="Global nitrogen regulator NrpR"
FT /id="PRO_0000106723"
FT REGION 12..77
FT /note="Winged helix-turn-helix"
FT /evidence="ECO:0000305"
FT REGION 85..320
FT /note="NRD 1"
FT /evidence="ECO:0000305|PubMed:21070950"
FT REGION 321..542
FT /note="NRD 2"
FT /evidence="ECO:0000305|PubMed:21070950"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:3NEK"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 346..355
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 450..462
FT /evidence="ECO:0007829|PDB:3NEK"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 523..532
FT /evidence="ECO:0007829|PDB:3NEK"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:3NEK"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3NEK"
SQ SEQUENCE 542 AA; 61195 MW; 5C7FC0734338AE0F CRC64;
MIIMADLDRK LIEILDILSK SKEPVGAKII AKELNKRGYK IGERAVRYHL KLLDGMKLTK
KVGYAGRVIT ERGLEELEKA NISYRLGSIY SNILEKTISA NYRFGYVVIN RCQVYADFND
VLKIIKSVYE SGLAVGDRVG IIDREKFVEI NTLCSLNFDN ILLQNGIFPL HVCAGVVKYE
DGKPVEFKEI IDYKSTSIDP LRAFIEKKET DVMGIIENGE GYLPANFRYF GVEFLERFET
ILEIDELKCI ISYGTENVLG LDVGDDKVGV ALIGGLTPIA PFVENNYCVE ICPMSSIVRL
ESLHKLKKNP RDIVTKKANI RIKTALSKMF NAMAKVTYDI DEADGDVIVN TAFIDKKYLD
EAFDILKEAY KKGLGISDRF GIVEENDRIK IQTICAVTLD GIFLRNSVPL IPKYGGILEI
TEDKERFIDI IGYDGSSLDP HEVFFNFVDC EKTFLAGFRE VHRVAREKLE EVLKKLNWNG
IKAIGEPNNE LYGIGVNKDM CGVVTMGGIN PLVLLKENEI PIELKAMHEV VRFSDLKSYK
EI
