GLNK1_METMA
ID GLNK1_METMA Reviewed; 117 AA.
AC Q8PYW7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nitrogen regulatory protein GlnK1 {ECO:0000305};
GN Name=glnK1 {ECO:0000303|PubMed:11807063};
GN OrderedLocusNames=MM_0732 {ECO:0000312|EMBL:AAM30428.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, SUBUNIT, INDUCTION, AND LACK OF URIDYLYLATION.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=11807063; DOI=10.1128/jb.184.4.1028-1040.2002;
RA Ehlers C., Grabbe R., Veit K., Schmitz R.A.;
RT "Characterization of GlnK1 from Methanosarcina mazei strain Goe1:
RT complementation of an Escherichia coli glnK mutant strain by GlnK1.";
RL J. Bacteriol. 184:1028-1040(2002).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH GLNA1.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=15752204; DOI=10.1111/j.1365-2958.2005.04511.x;
RA Ehlers C., Weidenbach K., Veit K., Forchhammer K., Schmitz R.A.;
RT "Unique mechanistic features of post-translational regulation of glutamine
RT synthetase activity in Methanosarcina mazei strain Goe1 in response to
RT nitrogen availability.";
RL Mol. Microbiol. 55:1841-1854(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=15824904; DOI=10.1007/s00438-005-1128-7;
RA Ehlers C., Weidenbach K., Veit K., Deppenmeier U., Metcalf W.W.,
RA Schmitz R.A.;
RT "Development of genetic methods and construction of a chromosomal glnK1
RT mutant in Methanosarcina mazei strain Goe1.";
RL Mol. Genet. Genomics 273:290-298(2005).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism
CC (PubMed:11807063). Regulates the activity of its targets by protein-
CC protein interaction in response to the nitrogen status of the cell
CC (PubMed:15752204, PubMed:15824904). Allows finetuning control of the
CC glutamine synthetase GlnA1 under changing nitrogen availabilities via
CC direct protein interaction (PubMed:15752204).
CC {ECO:0000269|PubMed:11807063, ECO:0000269|PubMed:15752204,
CC ECO:0000269|PubMed:15824904}.
CC -!- ACTIVITY REGULATION: Inhibitory effects on GlnA1 are abolished in the
CC presence of the effector 2-oxoglutarate. {ECO:0000269|PubMed:15752204}.
CC -!- SUBUNIT: Homotrimer (PubMed:11807063). Interacts and forms stable
CC complexes with the glutamine synthetase GlnA1 (PubMed:15752204).
CC {ECO:0000269|PubMed:11807063, ECO:0000269|PubMed:15752204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8ZYW0}.
CC -!- INDUCTION: Expressed under nitrogen-limiting conditions.
CC {ECO:0000269|PubMed:11807063}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant exhibits a partial growth
CC defect under nitrogen limitation when molecular nitrogen is used as the
CC sole nitrogen source. {ECO:0000269|PubMed:15824904}.
CC -!- MISCELLANEOUS: Unlike the enteric GlnK proteins, Glnk1 is not
CC covalently modified by uridylylation under nitrogen limitation.
CC {ECO:0000269|PubMed:11807063}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AE008384; AAM30428.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PYW7; -.
DR SMR; Q8PYW7; -.
DR STRING; 192952.MM_0732; -.
DR EnsemblBacteria; AAM30428; AAM30428; MM_0732.
DR KEGG; mma:MM_0732; -.
DR PATRIC; fig|192952.21.peg.869; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_0_2; -.
DR OMA; GVVMEVN; -.
DR Proteomes; UP000000595; 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 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; PS51343; PII_GLNB_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..117
FT /note="Nitrogen regulatory protein GlnK1"
FT /id="PRO_0000453017"
FT BINDING 32
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 40..42
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 40..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 92..95
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:O28524"
FT BINDING 92..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O28524"
SQ SEQUENCE 117 AA; 13054 MW; EC4DD3972C94F4BA CRC64;
MVAMKYVIAM IRPERLDAVK RELQKIEVSR LTVSSVSGYG AQKGYMEIYR AMEYDANLLE
KIKIEIAVND EFLEPTIEAI KTGAKGSDGY VGSGKIFVLP LENVIRIRTN ETGPEAI
