ID   GLNK_ECO57              Reviewed;         112 AA.
AC   P0AC57; P38504; P77118;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Z0562, ECs0504;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54800.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33927.1; -; Genomic_DNA.
DR   PIR; D85542; D85542.
DR   PIR; H90691; H90691.
DR   RefSeq; NP_308531.1; NC_002695.1.
DR   RefSeq; WP_000780338.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AC57; -.
DR   SMR; P0AC57; -.
DR   STRING; 155864.EDL933_0525; -.
DR   EnsemblBacteria; AAG54800; AAG54800; Z0562.
DR   EnsemblBacteria; BAB33927; BAB33927; ECs_0504.
DR   GeneID; 67416475; -.
DR   GeneID; 914607; -.
DR   KEGG; ece:Z0562; -.
DR   KEGG; ecs:ECs_0504; -.
DR   PATRIC; fig|386585.9.peg.609; -.
DR   eggNOG; COG0347; Bacteria.
DR   HOGENOM; CLU_082268_0_0_6; -.
DR   OMA; YRGTEHV; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein GlnK"
FT                   /id="PRO_0000139774"
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