GLNK_ECOL6
ID GLNK_ECOL6 Reviewed; 112 AA.
AC P0AC56; P38504; P77118;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Nitrogen regulatory protein GlnK {ECO:0000250|UniProtKB:P0AC55};
DE AltName: Full=Nitrogen regulatory protein P-II 2 {ECO:0000250|UniProtKB:P0AC55};
GN Name=glnK; OrderedLocusNames=c0568;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism. Regulates
CC the activity of its targets by protein-protein interaction in response
CC to the nitrogen status of the cell. Involved in the regulation of the
CC ammonium transporter AmtB so as to optimize ammonium uptake under all
CC growth conditions. In nitrogen-limited conditions, GlnK does not
CC interact with AmtB, which remains active and imports ammonium. When
CC extracellular ammonium increases, GlnK associates tightly with AmtB in
CC the inner membrane, thereby inhibiting the transporter activity.
CC {ECO:0000250|UniProtKB:P0AC55}.
CC -!- ACTIVITY REGULATION: Formation of the GlnK-AmtB complex is influenced
CC by intracellular pools of the effector molecules ATP, ADP, Mg(2+) and
CC 2-oxoglutarate. The GlnK-AmtB interaction is also controlled by the
CC level of intracellular glutamine and the uridylylation status of GlnK.
CC {ECO:0000250|UniProtKB:P0AC55}.
CC -!- SUBUNIT: Homotrimer. In response to elevation of the extracellular
CC ammonium concentration, interacts and forms a complex with AmtB.
CC {ECO:0000250|UniProtKB:P0AC55}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AC55}. Cell
CC inner membrane {ECO:0000250|UniProtKB:P0AC55}. Note=During nitrogen
CC limitation, GlnK is predominantly in its fully uridylylated state in
CC the cytoplasmic fraction. In response to nitrogen shock, GlnK is
CC deuridylylated rapidly and associates tightly with AmtB in the inner
CC membrane. {ECO:0000250|UniProtKB:P0AC55}.
CC -!- PTM: Uridylylated/deuridylylated by GlnD. Fully uridylylated in
CC nitrogen-limited conditions and deuridylylated when extracellular
CC ammonium increases. {ECO:0000250|UniProtKB:P0AC55}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AE014075; AAN79046.1; -; Genomic_DNA.
DR RefSeq; WP_000780338.1; NC_004431.1.
DR AlphaFoldDB; P0AC56; -.
DR SMR; P0AC56; -.
DR STRING; 199310.c0568; -.
DR EnsemblBacteria; AAN79046; AAN79046; c0568.
DR GeneID; 67416475; -.
DR KEGG; ecc:c0568; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_6; -.
DR OMA; YRGTEHV; -.
DR BioCyc; ECOL199310:C0568-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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 InterPro; IPR002332; N-reg_PII_urydylation_site.
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.
DR PROSITE; PS00496; PII_GLNB_UMP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein GlnK"
FT /id="PRO_0000139776"
FT BINDING 29
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 38..39
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 64
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 87..90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 87..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 101..103
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AC55"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12259 MW; 1875CD92C162B537 CRC64;
MKLVTVIIKP FKLEDVREAL SSIGIQGLTV TEVKGFGRQK GHAELYRGAE YSVNFLPKVK
IDVAIADDQL DEVIDIVSKA AYTGKIGDGK IFVAELQRVI RIRTGEADEA AL
