ID   GLNK2_METJA             Reviewed;         112 AA.
AC   Q58740;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Nitrogen regulatory protein GlnK2 {ECO:0000250|UniProtKB:Q60381};
GN   Name=glnK2 {ECO:0000305}; OrderedLocusNames=MJ1344;
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).
CC   -!- FUNCTION: Involved in the regulation of nitrogen metabolism (By
CC       similarity). Regulates the activity of its targets by protein-protein
CC       interaction in response to the nitrogen status of the cell (By
CC       similarity). Regulates the activity of the ammonia channel Amt2 via
CC       direct interaction (By similarity). {ECO:0000250|UniProtKB:Q60381}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts and forms a complex with
CC       Amt2 (By similarity). {ECO:0000250|UniProtKB:Q60381}.
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; AAB99353.1; -; Genomic_DNA.
DR   PIR; G64467; G64467.
DR   RefSeq; WP_010870862.1; NC_000909.1.
DR   AlphaFoldDB; Q58740; -.
DR   SMR; Q58740; -.
DR   STRING; 243232.MJ_1344; -.
DR   EnsemblBacteria; AAB99353; AAB99353; MJ_1344.
DR   GeneID; 1452247; -.
DR   KEGG; mja:MJ_1344; -.
DR   eggNOG; arCOG02305; Archaea.
DR   HOGENOM; CLU_082268_0_0_2; -.
DR   InParanoid; Q58740; -.
DR   OMA; YRGTEHV; -.
DR   OrthoDB; 113533at2157; -.
DR   PhylomeDB; Q58740; -.
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   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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein GlnK2"
FT                   /id="PRO_0000139816"
FT   BINDING         29
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         37..39
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         37..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         64
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         87..90
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
FT   BINDING         87..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O28524"
SQ   SEQUENCE   112 AA;  12532 MW;  3DDCE2A0F32FE9F3 CRC64;
     MKKVEAIIRP EKLEIVKKAL SDAGYVGMTV SEVKGRGVQG GIVERYRGRE YIVDLIPKVK
     IELVVKEEDV DNVIDIICEN ARTGNPGDGK IFVIPVERVV RVRTKEEGRD VL