ID   GLNB_PASMU              Reviewed;         112 AA.
AC   Q9CJK1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB; OrderedLocusNames=PM2004;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 by GlnE, so
CC       activating the enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- PTM: Uridylylated/deuridylylated by GlnD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
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DR   EMBL; AE004439; AAK04088.1; -; Genomic_DNA.
DR   RefSeq; WP_005725112.1; NC_002663.1.
DR   AlphaFoldDB; Q9CJK1; -.
DR   SMR; Q9CJK1; -.
DR   STRING; 747.DR93_2095; -.
DR   PRIDE; Q9CJK1; -.
DR   EnsemblBacteria; AAK04088; AAK04088; PM2004.
DR   GeneID; 62225943; -.
DR   KEGG; pmu:PM2004; -.
DR   HOGENOM; CLU_082268_0_0_6; -.
DR   OMA; HQIEVNF; -.
DR   Proteomes; UP000000809; Chromosome.
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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139781"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   112 AA;  12684 MW;  0CC9D24651F47642 CRC64;
     MKKIEAIIKP FKLDDVRESL SDVGITGMTV TEVRGFGRQK GHTELYRGAE YMVDFLPKVK
     MEIVVTDEQV DQCIEAIMET AQTGKIGDGK IFVYDVERVI RIRTGEENED AI