ID   GLNB_RHILV              Reviewed;         111 AA.
AC   P09827;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCC1001;
RX   PubMed=2882467; DOI=10.1093/nar/15.5.1951;
RA   Colonna-Romano S., Riccio A., Guida M., Defez R., Lamberti A.,
RA   Iaccarino M., Arnold W., Priefer U., Puehler A.;
RT   "Tight linkage of glnA and a putative regulatory gene in Rhizobium
RT   leguminosarum.";
RL   Nucleic Acids Res. 15:1951-1964(1987).
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   -!- 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; X04880; CAA28568.1; -; Genomic_DNA.
DR   PIR; B26567; B26567.
DR   AlphaFoldDB; P09827; -.
DR   SMR; P09827; -.
DR   PRIDE; P09827; -.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; 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   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..111
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139784"
FT   MOD_RES         50
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   111 AA;  12081 MW;  DA22BD0C3D66AF1D CRC64;
     MKKIEAIIKP FKLDEVRSPS GVGLQGITVT EAKGFGRQKG HTELYRGAEY VVDFLPKVKV
     EVVLADENAE AVIEAIRKAA QTGRIGDGKI FVSNVEEVIR IRTGETGIDA I