ID   GLNB_AQUAE              Reviewed;         112 AA.
AC   O66513;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB; OrderedLocusNames=aq_109;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2-
CC       ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP
CC       allows the deadenylation of glutamine synthetase (GS), thus activating
CC       the enzyme. Conversely, in nitrogen excess P-II is deuridylated and
CC       promotes the adenylation of GS. P-II indirectly controls the
CC       transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed
CC       conversion of NR-I to NR-I-phosphate, the transcriptional activator of
CC       glnA. When P-II is uridylylated to P-II-UMP, these events are reversed
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
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DR   EMBL; AE000657; AAC06473.1; -; Genomic_DNA.
DR   PIR; F70310; F70310.
DR   RefSeq; NP_213073.1; NC_000918.1.
DR   RefSeq; WP_010880011.1; NC_000918.1.
DR   PDB; 2EG1; X-ray; 1.80 A; A=1-112.
DR   PDB; 2EG2; X-ray; 1.72 A; A=1-112.
DR   PDB; 2Z0G; X-ray; 2.10 A; A/B/C/D=1-112.
DR   PDBsum; 2EG1; -.
DR   PDBsum; 2EG2; -.
DR   PDBsum; 2Z0G; -.
DR   AlphaFoldDB; O66513; -.
DR   SMR; O66513; -.
DR   STRING; 224324.aq_109; -.
DR   EnsemblBacteria; AAC06473; AAC06473; aq_109.
DR   KEGG; aae:aq_109; -.
DR   PATRIC; fig|224324.8.peg.94; -.
DR   eggNOG; COG0347; Bacteria.
DR   HOGENOM; CLU_082268_0_0_0; -.
DR   InParanoid; O66513; -.
DR   OMA; HQIEVNF; -.
DR   OrthoDB; 2021322at2; -.
DR   EvolutionaryTrace; O66513; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
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   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.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139768"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   HELIX           13..22
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:2Z0G"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:2EG2"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:2EG2"
SQ   SEQUENCE   112 AA;  12497 MW;  0E44B4B171A6233B CRC64;
     MKKIEAIIKP FKLDEVKDAL VEIGIGGMTV TEVKGFGQQK GHTEIYRGTE YVIDFLPKVK
     IEVVVRDEDV EKVVETIVKT AQTGRVGDGK IFIIPVEDVI RIRTGERGEQ AI