GLNB_BRADU
ID GLNB_BRADU Reviewed; 112 AA.
AC P14179;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Nitrogen regulatory protein P-II;
GN Name=glnB; OrderedLocusNames=blr4948;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2793830; DOI=10.1128/jb.171.10.5638-5645.1989;
RA Martin G.B., Thomashow M.F., Chelm B.K.;
RT "Bradyrhizobium japonicum glnB, a putative nitrogen-regulatory gene, is
RT regulated by NtrC at tandem promoters.";
RL J. Bacteriol. 171:5638-5645(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-111.
RX PubMed=2859270; DOI=10.1128/jb.162.2.698-703.1985;
RA Carlson T.A., Guerinot M.L., Chelm B.K.;
RT "Characterization of the gene encoding glutamine synthetase I (glnA) from
RT Bradyrhizobium japonicum.";
RL J. Bacteriol. 162:698-703(1985).
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; M26753; AAA26214.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC50213.1; -; Genomic_DNA.
DR EMBL; M10926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A33600; A33600.
DR RefSeq; NP_771588.1; NC_004463.1.
DR RefSeq; WP_007603495.1; NZ_CP011360.1.
DR AlphaFoldDB; P14179; -.
DR SMR; P14179; -.
DR STRING; 224911.27353213; -.
DR EnsemblBacteria; BAC50213; BAC50213; BAC50213.
DR GeneID; 66478575; -.
DR KEGG; bja:blr4948; -.
DR PATRIC; fig|224911.44.peg.4802; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_5; -.
DR InParanoid; P14179; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; P14179; -.
DR PRO; PR:P14179; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
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; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139770"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT CONFLICT 17..22
FT /note="KEALQE -> RSLSG (in Ref. 1; AAA26214)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="AE -> TD (in Ref. 1; AAA26214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12349 MW; 26BF924FB8FCE54C CRC64;
MKKIEAIIKP FKLDEVKEAL QEVGLQGITV TEAKGFGRQK GHAELYRGAE YIVDFLPKVK
IEIVIGDDLV ERAIDAIRRA AQTGRIGDGK IFVSNIEEAI RIRTGESGLD AI
