ID   GLNB_CYACA              Reviewed;         113 AA.
AC   Q9TM37;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
CC   -!- FUNCTION: P-II indirectly controls the transcription of the glutamine
CC       synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-
CC       I to NR-I-phosphate, the transcriptional activator of glnA. When P-II
CC       is uridylylated to P-II-UMP, these events are reversed. When the ratio
CC       of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP,
CC       which causes the deadenylation of glutamine synthetase, so activating
CC       the enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF022186; AAF13016.1; -; Genomic_DNA.
DR   RefSeq; NP_045029.1; NC_001840.1.
DR   AlphaFoldDB; Q9TM37; -.
DR   SMR; Q9TM37; -.
DR   GeneID; 800194; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Chloroplast; Nucleotide-binding; Phosphoprotein; Plastid; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..113
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139798"
FT   MOD_RES         52
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   113 AA;  12602 MW;  83C9468B2A3C83BC CRC64;
     MFSKLEAIIR PFKLEEVKVR LMTFGVPGIT VTNVMGCGKQ IGGIERSKGV EYDSELIEKV
     KIEIVVMNEH IDELIEIIIN AVWTGEIGDG KIFVSPVSSV IRIRTQDKDL DAI