GLNK1_METJA
ID GLNK1_METJA Reviewed; 112 AA.
AC Q60381;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Nitrogen regulatory protein GlnK1 {ECO:0000305};
GN Name=glnK1 {ECO:0000303|PubMed:17203075}; OrderedLocusNames=MJ0059;
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] {ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9D, ECO:0007744|PDB:2J9E}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEXES WITH ADP; AMP; ATP;
RP MAGNESIUM AND 2-OXOGLUTARATE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND
RP INTERACTION WITH AMT1.
RX PubMed=17203075; DOI=10.1038/sj.emboj.7601492;
RA Yildiz O., Kalthoff C., Raunser S., Kuhlbrandt W.;
RT "Structure of GlnK1 with bound effectors indicates regulatory mechanism for
RT ammonia uptake.";
RL EMBO J. 26:589-599(2007).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism
CC (PubMed:17203075). Regulates the activity of its targets by protein-
CC protein interaction in response to the nitrogen status of the cell
CC (PubMed:17203075). Regulates the activity of the ammonia channel Amt1
CC via direct interaction (PubMed:17203075).
CC {ECO:0000269|PubMed:17203075}.
CC -!- ACTIVITY REGULATION: Formation of the GlnK1/Amt1 complex is decreased
CC in the presence of Mg-ATP or 2-oxoglutarate. The presence of both
CC effectors abolishes the formation of the complex.
CC {ECO:0000269|PubMed:17203075}.
CC -!- SUBUNIT: Homotrimer (PubMed:17203075). Interacts and forms a complex
CC with Amt1 (PubMed:17203075). {ECO:0000269|PubMed:17203075}.
CC -!- INTERACTION:
CC Q60381; Q58739: amt2; NbExp=2; IntAct=EBI-7201321, EBI-7201308;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8ZYW0}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; L77117; AAB98041.1; -; Genomic_DNA.
DR PIR; C64307; C64307.
DR RefSeq; WP_010869551.1; NC_000909.1.
DR PDB; 2J9C; X-ray; 1.30 A; A/B/C=1-112.
DR PDB; 2J9D; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-112.
DR PDB; 2J9E; X-ray; 1.62 A; A/B/C=1-112.
DR PDB; 7P52; X-ray; 1.20 A; A=1-112.
DR PDBsum; 2J9C; -.
DR PDBsum; 2J9D; -.
DR PDBsum; 2J9E; -.
DR PDBsum; 7P52; -.
DR AlphaFoldDB; Q60381; -.
DR SMR; Q60381; -.
DR IntAct; Q60381; 1.
DR MINT; Q60381; -.
DR STRING; 243232.MJ_0059; -.
DR EnsemblBacteria; AAB98041; AAB98041; MJ_0059.
DR GeneID; 1450898; -.
DR KEGG; mja:MJ_0059; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_0_2; -.
DR InParanoid; Q60381; -.
DR OMA; HQIEVNF; -.
DR OrthoDB; 113533at2157; -.
DR PhylomeDB; Q60381; -.
DR EvolutionaryTrace; Q60381; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PIRSF; PIRSF039144; GlnB; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein GlnK1"
FT /id="PRO_0000139815"
FT BINDING 29
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9D"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E"
FT BINDING 52..54
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:17203075"
FT BINDING 64
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9D"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E"
FT BINDING 88..90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9D"
FT BINDING 101..103
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9D"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17203075,
FT ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7P52"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:7P52"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2J9D"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:7P52"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7P52"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:7P52"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2J9C"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7P52"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:7P52"
SQ SEQUENCE 112 AA; 12490 MW; 3DC3F307C32FE9F3 CRC64;
MKKVEAIIRP EKLEIVKKAL SDAGYVGMTV SEVKGRGVQG GIVERYRGRE YIVDLIPKVK
IELVVKEEDV DNVIDIICEN ARTGNPGDGK IFVIPVERVV RVRTKEEGKE AL
