GLNK2_HALMT
ID GLNK2_HALMT Reviewed; 123 AA.
AC B8ZYW1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Nitrogen regulatory protein GlnK2 {ECO:0000305};
GN Name=glnK2 {ECO:0000303|PubMed:21265784};
GN OrderedLocusNames=HFX_0092 {ECO:0000312|EMBL:AFK17834.1};
GN ORFNames=BM92_08825 {ECO:0000312|EMBL:AHZ22740.1},
GN C439_09930 {ECO:0000312|EMBL:EMA02893.1},
GN E6P09_03555 {ECO:0000312|EMBL:QCQ74395.1};
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, AND SUBCELLULAR LOCATION.
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-62.
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 INTERACTION WITH AMT1, AND INDUCTION.
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).
RN [9] {ECO:0007744|PDB:4OZJ, ECO:0007744|PDB:4OZL, ECO:0007744|PDB:4OZN}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH ADP; AMP AND ATP,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=24946894; DOI=10.1111/febs.12881;
RA Palanca C., Pedro-Roig L., Llacer J.L., Camacho M., Bonete M.J., Rubio V.;
RT "The structure of a PII signaling protein from a halophilic archaeon
RT reveals novel traits and high-salt adaptations.";
RL FEBS J. 281:3299-3314(2014).
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:23069245). Increases the activity of the
CC glutamine synthetase 3 in the presence of 2-oxoglutarate
CC (PubMed:23069245). May regulate the activity of the ammonia channel
CC Amt2 via direct interaction (By similarity).
CC {ECO:0000250|UniProtKB:B8ZYW0, ECO:0000269|PubMed:21265784,
CC ECO:0000269|PubMed:23069245, ECO:0000269|PubMed:23420616}.
CC -!- ACTIVITY REGULATION: Binds the effectors ADP and ATP. Also binds AMP
CC with high affinity, raising the possibility that AMP could be an
CC important PII effector, at least in archaea. The change in the ATP/AMP
CC ratio may be more relevant for describing the energy status in the
CC cells than the ATP/ADP ratio alone. {ECO:0000269|PubMed:24946894}.
CC -!- SUBUNIT: Homotrimer (PubMed:23069245, PubMed:24946894). Interacts with
CC the glutamine synthetase 3 (GS3) in the presence of 2-oxoglutarate
CC (PubMed:23069245). Interacts in vitro with Amt1 after ammonium shock
CC (PubMed:24039236). May also interact with Amt2 (PubMed:24039236).
CC {ECO:0000269|PubMed:23069245, ECO:0000269|PubMed:24039236,
CC ECO:0000269|PubMed:24946894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21265784}.
CC -!- INDUCTION: Expressed during ammonium starvation under nitrate-rich
CC conditions. {ECO:0000269|PubMed:24039236}.
CC -!- PTM: Uridylylated on Tyr-62. {ECO:0000269|PubMed:23420616}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; FM991872; CAX20371.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK17834.1; -; Genomic_DNA.
DR EMBL; AOLO01000007; EMA02893.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ22740.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ74395.1; -; Genomic_DNA.
DR PDB; 4OZJ; X-ray; 1.45 A; A=1-123.
DR PDB; 4OZL; X-ray; 1.49 A; A=1-119.
DR PDB; 4OZN; X-ray; 2.60 A; A/B/C=1-123.
DR PDBsum; 4OZJ; -.
DR PDBsum; 4OZL; -.
DR PDBsum; 4OZN; -.
DR AlphaFoldDB; B8ZYW1; -.
DR SMR; B8ZYW1; -.
DR MINT; B8ZYW1; -.
DR STRING; 523841.HFX_0092; -.
DR EnsemblBacteria; AFK17834; AFK17834; HFX_0092.
DR EnsemblBacteria; AHZ22740; AHZ22740; BM92_08825.
DR EnsemblBacteria; EMA02893; EMA02893; C439_09930.
DR EnsemblBacteria; QCQ74395; QCQ74395; E6P09_03555.
DR KEGG; hme:HFX_0092; -.
DR PATRIC; fig|523841.21.peg.2019; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_1_2; -.
DR OMA; YRGTEHV; -.
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 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..123
FT /note="Nitrogen regulatory protein GlnK2"
FT /id="PRO_0000453016"
FT BINDING 38..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4OZN"
FT BINDING 49
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4OZJ"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4OZJ"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4OZN"
FT BINDING 98..101
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4OZJ"
FT BINDING 98..101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:4OZL"
FT BINDING 98..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4OZN"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4OZN"
FT MOD_RES 62
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675,
FT ECO:0000269|PubMed:23420616"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4OZJ"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:4OZJ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4OZJ"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:4OZJ"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4OZJ"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:4OZN"
FT STRAND 67..79
FT /evidence="ECO:0007829|PDB:4OZJ"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:4OZJ"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4OZJ"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4OZN"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4OZJ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4OZJ"
SQ SEQUENCE 123 AA; 12921 MW; 5C1E0038524F2382 CRC64;
MSDADLPNDG GIKLVMAIIR PDKLADVKTA LAEVGAPSLT VTNVSGRGSQ PAKKSQWRGE
EYTVDLHQKV KVECVVADTP AEDVADAIAD AAHTGEKGDG KIFILPVENA IQVRTGKTGR
DAV
