GLNB_RHILO
ID GLNB_RHILO Reviewed; 112 AA.
AC Q98N18;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Nitrogen regulatory protein P-II;
GN Name=glnB; OrderedLocusNames=mll0345;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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}.
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DR EMBL; BA000012; BAB47945.1; -; Genomic_DNA.
DR RefSeq; WP_006205430.1; NC_002678.2.
DR AlphaFoldDB; Q98N18; -.
DR SMR; Q98N18; -.
DR STRING; 266835.14021332; -.
DR PRIDE; Q98N18; -.
DR EnsemblBacteria; BAB47945; BAB47945; BAB47945.
DR GeneID; 66684176; -.
DR KEGG; mlo:mll0345; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_5; -.
DR OMA; YRGTEHV; -.
DR OrthoDB; 2021322at2; -.
DR Proteomes; UP000000552; 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 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..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139783"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12200 MW; CF0F60FE7185465A CRC64;
MKKIEAIIKP FKLDEVKEAL QEAGLQGITV TEAKGFGRQK GHTELYRGAE YVVDFLPKVK
IEVVLGDDAV EGAIEAIRKA AQTGRIGDGK IFVSNIEEVV RIRTGETGMD AV
