GLNK2_ARCFU
ID GLNK2_ARCFU Reviewed; 112 AA.
AC O28527;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nitrogen regulatory protein GlnK2 {ECO:0000305};
DE AltName: Full=Af-GlnK-2 {ECO:0000303|PubMed:20643148};
GN Name=glnK2 {ECO:0000303|PubMed:20643148};
GN OrderedLocusNames=AF_1747 {ECO:0000312|EMBL:AAB89507.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP MUTAGENESIS OF PRO-86.
RX PubMed=22039461; DOI=10.1371/journal.pone.0026327;
RA Maier S., Schleberger P., Lu W., Wacker T., Pfluger T., Litz C.,
RA Andrade S.L.;
RT "Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing
RT of 2-oxoglutarate.";
RL PLoS ONE 6:e26327-e26327(2011).
RN [3] {ECO:0007744|PDB:3NCP, ECO:0007744|PDB:3NCQ, ECO:0007744|PDB:3NCR}
RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEXES WITH ADP AND ATP,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=20643148; DOI=10.1016/j.jmb.2010.07.020;
RA Helfmann S., Lu W., Litz C., Andrade S.L.;
RT "Cooperative binding of MgATP and MgADP in the trimeric P(II) protein GlnK2
RT from Archaeoglobus fulgidus.";
RL J. Mol. Biol. 402:165-177(2010).
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 -!- ACTIVITY REGULATION: Binding of adenosine nucleotides results in
CC distinct, cooperative behavior for ATP and ADP. GlnK2 is completely
CC insensitive to 2-oxoglutarate at a low level of intracellular nitrogen.
CC {ECO:0000269|PubMed:20643148}.
CC -!- SUBUNIT: Homotrimer (PubMed:20643148). Interacts and forms a complex
CC with Amt2 (By similarity). {ECO:0000250|UniProtKB:Q60381,
CC ECO:0000269|PubMed:20643148}.
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; AE000782; AAB89507.1; -; Genomic_DNA.
DR PIR; B69468; B69468.
DR RefSeq; WP_010879243.1; NC_000917.1.
DR PDB; 3NCP; X-ray; 2.35 A; A/B/C/D=1-112.
DR PDB; 3NCQ; X-ray; 1.24 A; A/B/C=1-112.
DR PDB; 3NCR; X-ray; 1.44 A; A/B/C=1-112.
DR PDBsum; 3NCP; -.
DR PDBsum; 3NCQ; -.
DR PDBsum; 3NCR; -.
DR AlphaFoldDB; O28527; -.
DR SMR; O28527; -.
DR STRING; 224325.AF_1747; -.
DR EnsemblBacteria; AAB89507; AAB89507; AF_1747.
DR GeneID; 24795491; -.
DR KEGG; afu:AF_1747; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_0_2; -.
DR OMA; DLAPQIV; -.
DR OrthoDB; 113533at2157; -.
DR PhylomeDB; O28527; -.
DR EvolutionaryTrace; O28527; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
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 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 GlnK2"
FT /id="PRO_0000453013"
FT BINDING 29
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCR"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCQ"
FT BINDING 38..39
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCR"
FT BINDING 38..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCQ"
FT BINDING 64
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCR"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCQ"
FT BINDING 87..90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCR"
FT BINDING 87..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCQ"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20643148,
FT ECO:0007744|PDB:3NCQ"
FT MUTAGEN 86
FT /note="P->F,I: Does not confer the ability to bind 2-
FT oxoglutarate."
FT /evidence="ECO:0000269|PubMed:22039461"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3NCQ"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3NCQ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:3NCQ"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3NCQ"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:3NCQ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3NCQ"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:3NCQ"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3NCQ"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3NCQ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3NCQ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3NCQ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3NCQ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3NCQ"
SQ SEQUENCE 112 AA; 12320 MW; BFA303FC72409D31 CRC64;
MKKIEAIVRA EKFPEVKAAL EERGFYGMTV TDVKGRGQQG GMQIQFRGRT MEVTLLPKVK
LEIVVKDDAV EEVIGLIVNS AFTGSPGDGK IFIIPVEDVV RIRTGERGDD SL
