ID   GLNB_RHIEC              Reviewed;         112 AA.
AC   O54053; Q2K367;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB; Synonyms=glnK; OrderedLocusNames=RHE_CH03974;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE3;
RX   PubMed=9487694; DOI=10.1094/mpmi.1998.11.3.188;
RA   Tate R., Riccio A., Merrick M., Patriarca E.J.;
RT   "The Rhizobium etli amtB gene coding for an NH4+ transporter is down-
RT   regulated early during bacteroid differentiation.";
RL   Mol. Plant Microbe Interact. 11:188-198(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ002489; CAA05496.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000133; ABC92719.1; -; Genomic_DNA.
DR   RefSeq; WP_007632398.1; NC_007761.1.
DR   AlphaFoldDB; O54053; -.
DR   SMR; O54053; -.
DR   STRING; 347834.RHE_CH03974; -.
DR   PRIDE; O54053; -.
DR   EnsemblBacteria; ABC92719; ABC92719; RHE_CH03974.
DR   GeneID; 61482416; -.
DR   GeneID; 66148229; -.
DR   KEGG; ret:RHE_CH03974; -.
DR   eggNOG; COG0347; Bacteria.
DR   HOGENOM; CLU_082268_0_0_5; -.
DR   OMA; LEMAIHT; -.
DR   Proteomes; UP000001936; Chromosome.
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   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.
PE   3: Inferred from homology;
KW   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139782"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT   CONFLICT        50
FT                   /note="E -> V (in Ref. 1; CAA05496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="A -> G (in Ref. 1; CAA05496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   112 AA;  12178 MW;  DFAE526476C82DA3 CRC64;
     MKIVMAIIKP FKLDEVREAL TAIGIQGLTV TEVKGYGRQK GHTEIYRGTE YAVSFLPKLK
     IEIAVASELV DRAVEAIAAS AKTGQIGDGK IFVYSIDHAV RIRTGETDSE AL