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GLNK2_ARCFU
ID   GLNK2_ARCFU             Reviewed;         112 AA.
AC   O28527;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Nitrogen regulatory protein GlnK2 {ECO:0000305};
DE   AltName: Full=Af-GlnK-2 {ECO:0000303|PubMed:20643148};
GN   Name=glnK2 {ECO:0000303|PubMed:20643148};
GN   OrderedLocusNames=AF_1747 {ECO:0000312|EMBL:AAB89507.1};
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   MUTAGENESIS OF PRO-86.
RX   PubMed=22039461; DOI=10.1371/journal.pone.0026327;
RA   Maier S., Schleberger P., Lu W., Wacker T., Pfluger T., Litz C.,
RA   Andrade S.L.;
RT   "Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing
RT   of 2-oxoglutarate.";
RL   PLoS ONE 6:e26327-e26327(2011).
RN   [3] {ECO:0007744|PDB:3NCP, ECO:0007744|PDB:3NCQ, ECO:0007744|PDB:3NCR}
RP   X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEXES WITH ADP AND ATP,
RP   ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=20643148; DOI=10.1016/j.jmb.2010.07.020;
RA   Helfmann S., Lu W., Litz C., Andrade S.L.;
RT   "Cooperative binding of MgATP and MgADP in the trimeric P(II) protein GlnK2
RT   from Archaeoglobus fulgidus.";
RL   J. Mol. Biol. 402:165-177(2010).
CC   -!- FUNCTION: Involved in the regulation of nitrogen metabolism (By
CC       similarity). Regulates the activity of its targets by protein-protein
CC       interaction in response to the nitrogen status of the cell (By
CC       similarity). Regulates the activity of the ammonia channel Amt2 via
CC       direct interaction (By similarity). {ECO:0000250|UniProtKB:Q60381}.
CC   -!- ACTIVITY REGULATION: Binding of adenosine nucleotides results in
CC       distinct, cooperative behavior for ATP and ADP. GlnK2 is completely
CC       insensitive to 2-oxoglutarate at a low level of intracellular nitrogen.
CC       {ECO:0000269|PubMed:20643148}.
CC   -!- SUBUNIT: Homotrimer (PubMed:20643148). Interacts and forms a complex
CC       with Amt2 (By similarity). {ECO:0000250|UniProtKB:Q60381,
CC       ECO:0000269|PubMed:20643148}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8ZYW0}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
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DR   EMBL; AE000782; AAB89507.1; -; Genomic_DNA.
DR   PIR; B69468; B69468.
DR   RefSeq; WP_010879243.1; NC_000917.1.
DR   PDB; 3NCP; X-ray; 2.35 A; A/B/C/D=1-112.
DR   PDB; 3NCQ; X-ray; 1.24 A; A/B/C=1-112.
DR   PDB; 3NCR; X-ray; 1.44 A; A/B/C=1-112.
DR   PDBsum; 3NCP; -.
DR   PDBsum; 3NCQ; -.
DR   PDBsum; 3NCR; -.
DR   AlphaFoldDB; O28527; -.
DR   SMR; O28527; -.
DR   STRING; 224325.AF_1747; -.
DR   EnsemblBacteria; AAB89507; AAB89507; AF_1747.
DR   GeneID; 24795491; -.
DR   KEGG; afu:AF_1747; -.
DR   eggNOG; arCOG02305; Archaea.
DR   HOGENOM; CLU_082268_0_0_2; -.
DR   OMA; DLAPQIV; -.
DR   OrthoDB; 113533at2157; -.
DR   PhylomeDB; O28527; -.
DR   EvolutionaryTrace; O28527; -.
DR   Proteomes; UP000002199; 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;
KW   Reference proteome.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein GlnK2"
FT                   /id="PRO_0000453013"
FT   BINDING         29
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCR"
FT   BINDING         29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCQ"
FT   BINDING         38..39
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCR"
FT   BINDING         38..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCQ"
FT   BINDING         64
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCR"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCQ"
FT   BINDING         87..90
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCR"
FT   BINDING         87..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCQ"
FT   BINDING         101..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20643148,
FT                   ECO:0007744|PDB:3NCQ"
FT   MUTAGEN         86
FT                   /note="P->F,I: Does not confer the ability to bind 2-
FT                   oxoglutarate."
FT                   /evidence="ECO:0000269|PubMed:22039461"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   HELIX           13..22
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   TURN            39..42
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:3NCQ"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:3NCQ"
SQ   SEQUENCE   112 AA;  12320 MW;  BFA303FC72409D31 CRC64;
     MKKIEAIVRA EKFPEVKAAL EERGFYGMTV TDVKGRGQQG GMQIQFRGRT MEVTLLPKVK
     LEIVVKDDAV EEVIGLIVNS AFTGSPGDGK IFIIPVEDVV RIRTGERGDD SL
 
 
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