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IID90048
UniprotP0AC55
ProteinNitrogen regulatory protein GlnK
GeneglnK
OrganismEscherichia coli (strain K12)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
112
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-112 Monomer :
 Evidence X-RAY 2gnk A Reference
       Region 2gnk A 1-37 order
       Region 2gnk A 38-54 disorder
       Region 2gnk A 55-112 order
Seq 1-112 Hetero hexamer : P69681
 Evidence X-RAY 2ns1 B Reference
       Region 2ns1 B 1-112 order
 Evidence X-RAY 2nuu G Reference
       Region 2nuu G 1-112 order
 Evidence X-RAY 2nuu H Reference
       Region 2nuu H 1-112 order
 Evidence X-RAY 2nuu I Reference
       Region 2nuu I 1-112 order
 Evidence X-RAY 2nuu J Reference
       Region 2nuu J 1-112 order
 Evidence X-RAY 2nuu K Reference
       Region 2nuu K 1-112 order
 Evidence X-RAY 2nuu L Reference
       Region 2nuu L 1-112 order
Seq 1-112 Homo trimer :
 Evidence X-RAY 1gnk A Reference
       Region 1gnk A 1-38 order
       Region 1gnk A 39-52 disorder
       Region 1gnk A 53-112 order
 Evidence X-RAY 1gnk B Reference
       Region 1gnk B 1-112 order
SeqProS verified 38-54 Hetero hexamer : P69681
       Region 2nuu G 1-112 order
       Region 2nuu H 1-112 order
       Region 2nuu I 1-112 order
       Region 2nuu J 1-112 order
       Region 2nuu K 1-112 order
       Region 2nuu L 1-112 order
       Region 2ns1 B 1-112 order
       Region 2gnk A 38-54 disorder
 
Prediction
NeProc
Disorder 109-112
Order 1-108
ProS 109-112
AlphaFold
Disorder 40-45,50-53
Order 1-39,46-49,54-112
Function
Function in SwissProt
Involved in the regulation of nitrogen metabolism (PubMed:8843440, PubMed:10760266, PubMed:11847102, PubMed:12366843, PubMed:14668330, PubMed:28538158). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (PubMed:8843440, PubMed:10760266, PubMed:11847102, PubMed:14668330). Involved in the regulation of the ammonium transporter AmtB so as to optimize ammonium uptake under all growth conditions (PubMed:11847102, PubMed:14668330, PubMed:16864585). In nitrogen-limited conditions, GlnK does not interact with AmtB, which remains active and imports ammonium. When extracellular ammonium increases, GlnK associates tightly with AmtB in the inner membrane, thereby inhibiting the transporter activity (PubMed:11847102, PubMed:14668330, PubMed:16864585). Also involved in the regulation of the glutamine synthetase adenylyltransferase/adenylyl-removing (AT/AR) enzyme GlnE and the glutamine synthetase GlnA (PubMed:8843440, PubMed:10760266, PubMed:28538158). In nitrogen-limited conditions, formation of uridylylated GlnB(PII)/GlnK heterotrimers may fine-regulate the activation of GlnA: uridylylated heterotrimers stimulate the deadenylation and the activation of GlnA whereas uridylylated GlnK homotrimers do not stimulate, or hardly stimulate, the deadenylation of GlnA (PubMed:10760266). In addition, regulates the expression of Ntr genes during nitrogen starvation, probably via the control of the levels of phosphorylated NRI during different stages of the response to nitrogen limitation (PubMed:12366843).