GLNB_NOSP7
ID GLNB_NOSP7 Reviewed; 112 AA.
AC O30794; B2IUQ8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Nitrogen regulatory protein P-II;
DE AltName: Full=PII signal transducing protein;
GN Name=glnB; OrderedLocusNames=Npun_F4466;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9639924; DOI=10.1099/00221287-144-6-1537;
RA Hanson T.E., Forchhammer K., Tandeau de Marsac N., Meeks J.C.;
RT "Characterization of the glnB gene product of Nostoc punctiforme strain
RT ATCC 29133: glnB or the PII protein may be essential.";
RL Microbiology 144:1537-1547(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: P-II indirectly controls the transcription of the GS gene
CC (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-
CC phosphate, the transcriptional activator of glnA. When P-II is
CC phosphorylated, these events are reversed. In nitrogen-limiting
CC conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is
CC phosphorylated which allows the deadenylation of glutamine synthetase
CC (GS), thus activating the enzyme (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- PTM: Phosphorylation dependent on the nitrogen source and spectral
CC light quality. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AF017419; AAC26348.1; -; Genomic_DNA.
DR EMBL; CP001037; ACC82833.1; -; Genomic_DNA.
DR RefSeq; WP_012410794.1; NC_010628.1.
DR AlphaFoldDB; O30794; -.
DR SMR; O30794; -.
DR STRING; 63737.Npun_F4466; -.
DR EnsemblBacteria; ACC82833; ACC82833; Npun_F4466.
DR GeneID; 57097222; -.
DR KEGG; npu:Npun_F4466; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_3; -.
DR OMA; HQIEVNF; -.
DR OrthoDB; 2021322at2; -.
DR PhylomeDB; O30794; -.
DR Proteomes; UP000001191; 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_0000139797"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12479 MW; 9C2224C38B67583A CRC64;
MKKVEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK
VEIVVDDNQV DMVVDKIIAA ARTGEIGDGK IFISPVEQVI RIRTGEKNTE AV