GLNK1_ARCFU
ID GLNK1_ARCFU Reviewed; 120 AA.
AC O29284;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Nitrogen regulatory protein GlnK1 {ECO:0000305};
GN Name=glnK1 {ECO:0000303|PubMed:21301082};
GN OrderedLocusNames=AF_0978 {ECO:0000312|EMBL:AAB90263.1};
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] {ECO:0007744|PDB:3O8W}
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 12-120, AND SUBUNIT.
RX PubMed=21301082; DOI=10.1107/s1744309110047482;
RA Litz C., Helfmann S., Gerhardt S., Andrade S.L.;
RT "Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus.";
RL Acta Crystallogr. F Struct. Biol. Commun. 67:178-181(2011).
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 Amt1 via
CC direct interaction (By similarity). {ECO:0000250|UniProtKB:Q60381}.
CC -!- SUBUNIT: Homotrimer (PubMed:21301082). Interacts and forms a complex
CC with Amt1 (By similarity). {ECO:0000250|UniProtKB:Q60381,
CC ECO:0000269|PubMed:21301082}.
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; AAB90263.1; -; Genomic_DNA.
DR PIR; B69372; B69372.
DR PDB; 3O8W; X-ray; 2.28 A; A=12-120.
DR PDBsum; 3O8W; -.
DR AlphaFoldDB; O29284; -.
DR SMR; O29284; -.
DR STRING; 224325.AF_0978; -.
DR EnsemblBacteria; AAB90263; AAB90263; AF_0978.
DR KEGG; afu:AF_0978; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_1_2; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; O29284; -.
DR EvolutionaryTrace; O29284; -.
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..120
FT /note="Nitrogen regulatory protein GlnK1"
FT /id="PRO_0000453012"
FT BINDING 40
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 48..50
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 48..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 75
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 98..101
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 98..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3O8W"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3O8W"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3O8W"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3O8W"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3O8W"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:3O8W"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3O8W"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3O8W"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3O8W"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3O8W"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3O8W"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3O8W"
SQ SEQUENCE 120 AA; 13484 MW; 8B811B4C45704E9A CRC64;
MRRLPTREVV EMKMVVAVIR PEKLECVKKA LEERGFVGMT VTEVKGRGEQ KGIRLQFRGR
EVEVDLLQKT KVEVVVSDDA VDEVVEAIVS SARTGKFGDG RIFVIPVEKS VKIRTGEEEV
