ID   GLNB_MICDP              Reviewed;         112 AA.
AC   Q47894;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Nitrogen regulatory protein P-II;
DE   AltName: Full=PII signal transducing protein;
GN   Name=glnB;
OS   Microchaete diplosiphon (Fremyella diplosiphon).
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX   NCBI_TaxID=1197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Liotenberg S., Castets A.M., Campbell D., Houmard J., Tandeau de Marsac N.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: P-II indirectly controls the transcription of the GS gene
CC       (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-
CC       phosphate, the transcriptional activator of glnA. When P-II is
CC       phosphorylated, these events are reversed. In nitrogen-limiting
CC       conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is
CC       phosphorylated which allows the deadenylation of glutamine synthetase
CC       (GS), thus activating the enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- PTM: Phosphorylation dependent on the nitrogen source and spectral
CC       light quality. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
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DR   EMBL; X97327; CAA65992.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47894; -.
DR   SMR; Q47894; -.
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   InterPro; IPR002332; N-reg_PII_urydylation_site.
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.
DR   PROSITE; PS00496; PII_GLNB_UMP; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139796"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   112 AA;  12479 MW;  F74E54C393C4596B CRC64;
     MKKVEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK
     VEIVVEDNQV DMVVDKIIAA ARTGEIGDGK IFISPVEQVV RIRTGEKNTE AV