ID   GLNB_KLEOX              Reviewed;         112 AA.
AC   P11671;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLU-50.
RC   STRAIN=M5a1;
RX   PubMed=2907369; DOI=10.1007/bf00331314;
RA   Holtel A., Merrick M.;
RT   "Identification of the Klebsiella pneumoniae glnB gene: nucleotide sequence
RT   of wild-type and mutant alleles.";
RL   Mol. Gen. Genet. 215:134-138(1988).
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; X14012; CAA32177.1; -; Genomic_DNA.
DR   PIR; S04377; S04377.
DR   RefSeq; WP_002914032.1; NZ_WVTN01000003.1.
DR   AlphaFoldDB; P11671; -.
DR   SMR; P11671; -.
DR   STRING; 571.MC52_29370; -.
DR   GeneID; 64336189; -.
DR   GeneID; 67516283; -.
DR   eggNOG; COG0347; Bacteria.
DR   OrthoDB; 2021322at2; -.
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   1: Evidence at protein level;
KW   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139778"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT   MUTAGEN         50
FT                   /note="E->Y: Glutamine auxotrophy."
FT                   /evidence="ECO:0000269|PubMed:2907369"
SQ   SEQUENCE   112 AA;  12429 MW;  CC15D58A2F225507 CRC64;
     MKKIDAIIKP FKLDDVREAL AEVGITGMTV TEVKGFGRQK GHTELYRGAE YMVDFLPKVK
     IEIVVTDDIV DTCVDTIIRT AQTGKIGDGK IFVFDVARVI RIRTGEEDDA AI