GLNK1_HALMT
ID GLNK1_HALMT Reviewed; 122 AA.
AC B8ZYW0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Nitrogen regulatory protein GlnK1 {ECO:0000305};
GN Name=glnK1 {ECO:0000303|PubMed:21265784};
GN OrderedLocusNames=HFX_0094 {ECO:0000312|EMBL:AFK17836.1};
GN ORFNames=BM92_08810 {ECO:0000312|EMBL:AHZ22738.1},
GN C439_09920 {ECO:0000312|EMBL:EMA02891.1},
GN E6P09_03565 {ECO:0000312|EMBL:QCQ74397.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=21265784; DOI=10.1042/bst0390259;
RA Pedro-Roig L., Camacho M., Bonete M.J.;
RT "In vitro proof of direct regulation of glutamine synthetase by GlnK
RT proteins in the extreme halophilic archaeon Haloferax mediterranei.";
RL Biochem. Soc. Trans. 39:259-262(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH GLNA3.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=23069245; DOI=10.1016/j.bbapap.2012.10.006;
RA Pedro-Roig L., Camacho M., Bonete M.J.;
RT "Regulation of ammonium assimilation in Haloferax mediterranei: interaction
RT between glutamine synthetase and two GlnK proteins.";
RL Biochim. Biophys. Acta 1834:16-23(2013).
RN [7]
RP FUNCTION, AND URIDYLYLATION AT TYR-61.
RX PubMed=23420616; DOI=10.1002/pmic.201200465;
RA Pedro-Roig L., Camacho M., Bonete M.J.;
RT "Haloferax mediterranei GlnK proteins are post-translationally modified by
RT uridylylation.";
RL Proteomics 13:1371-1374(2013).
RN [8]
RP FUNCTION, INTERACTION WITH AMT1, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=24039236; DOI=10.1002/mbo3.120;
RA Pedro-Roig L., Lange C., Bonete M.J., Soppa J., Maupin-Furlow J.;
RT "Nitrogen regulation of protein-protein interactions and transcript levels
RT of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.";
RL MicrobiologyOpen 2:826-840(2013).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism
CC (PubMed:21265784, PubMed:23420616). Regulates the activity of its
CC targets by protein-protein interaction in response to the nitrogen
CC status of the cell (PubMed:24039236, PubMed:23069245). Increases the
CC activity of the glutamine synthetase 3 in the presence of 2-
CC oxoglutarate (PubMed:23069245). May regulate the activity of the
CC ammonia channel Amt1 via direct interaction (PubMed:24039236).
CC {ECO:0000269|PubMed:21265784, ECO:0000269|PubMed:23069245,
CC ECO:0000269|PubMed:23420616, ECO:0000269|PubMed:24039236}.
CC -!- SUBUNIT: Homotrimer (PubMed:23069245). Interacts with the glutamine
CC synthetase 3 (GS3) in the presence of 2-oxoglutarate (PubMed:23069245).
CC Interacts with Amt1 after ammonium shock (PubMed:24039236).
CC {ECO:0000269|PubMed:23069245, ECO:0000269|PubMed:24039236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21265784}.
CC -!- INDUCTION: Highly expressed during ammonium starvation under nitrate-
CC rich conditions. {ECO:0000269|PubMed:21265784,
CC ECO:0000269|PubMed:24039236}.
CC -!- PTM: Uridylylated on Tyr-61. {ECO:0000269|PubMed:23420616}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows growth deficiency in medium
CC supplemented with nitrate. {ECO:0000269|PubMed:24039236}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; FM991871; CAX20370.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK17836.1; -; Genomic_DNA.
DR EMBL; AOLO01000007; EMA02891.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ22738.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ74397.1; -; Genomic_DNA.
DR AlphaFoldDB; B8ZYW0; -.
DR SMR; B8ZYW0; -.
DR STRING; 523841.HFX_0094; -.
DR EnsemblBacteria; AFK17836; AFK17836; HFX_0094.
DR EnsemblBacteria; AHZ22738; AHZ22738; BM92_08810.
DR EnsemblBacteria; EMA02891; EMA02891; C439_09920.
DR EnsemblBacteria; QCQ74397; QCQ74397; E6P09_03565.
DR KEGG; hme:HFX_0094; -.
DR PATRIC; fig|523841.21.peg.2017; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_0_2; -.
DR OMA; HQIEVNF; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; 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 ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..122
FT /note="Nitrogen regulatory protein GlnK1"
FT /id="PRO_0000453015"
FT BINDING 39
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 47..49
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 47..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 74
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 97..100
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 97..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT MOD_RES 61
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675,
FT ECO:0000269|PubMed:23420616"
SQ SEQUENCE 122 AA; 12705 MW; 6783420FC1948653 CRC64;
MSETETGNDG IKLVMAIIRP DKLADVKTAL AEVGAPSLTV TNVSGRGSQP AKKGQWRGEE
YTVDLHQKVK IECVVADIPA GDVVDAIAEA AHTGEKGDGK IFILPVEGAV QVRTGKEGSP
AV
