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P0A3F4 (GLNB_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nitrogen regulatory protein P-II
Alternative name(s):
PII signal transducing protein
Gene names
Name:glnB
Ordered Locus Names:Synpcc7942_0321
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length112 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.

Subunit structure

Homotrimer.

Post-translational modification

Phosphorylation dependent on the nitrogen source and spectral light quality.

Sequence similarities

Belongs to the P(II) protein family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-700889,EBI-700889
argBQ6V1L56EBI-700889,EBI-700898

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 112112Nitrogen regulatory protein P-II
PRO_0000139794

Amino acid modifications

Modified residue491Phosphoserine Ref.4
Modified residue511O-UMP-tyrosine By similarity

Experimental info

Sequence conflict831T → P in AAA27312. Ref.1

Secondary structure

........................... 112
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A3F4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5F44B64CBFF3C559

FASTA11212,391
        10         20         30         40         50         60 
MKKIEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK 

        70         80         90        100        110 
LEIVVEDAQV DTVIDKIVAA ARTGEIGDGK IFVSPVDQTI RIRTGEKNAD AI 

« Hide

References

« Hide 'large scale' references
[1]"Photosynthetic electron transport controls nitrogen assimilation in cyanobacteria by means of posttranslational modification of the glnB gene product."
Tsinoremas N.F., Castets A.M., Harrison M.A., Allen J.F., Tandeau de Marsac N.
Proc. Natl. Acad. Sci. U.S.A. 88:4565-4569(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.
[3]"The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status."
Forchhammer K., Tandeau de Marsac N.
J. Bacteriol. 176:84-91(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[4]"Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity."
Forchhammer K., Tandeau de Marsac N.
J. Bacteriol. 177:5812-5817(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-49.
[5]"The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803."
Xu Y., Carr P.D., Clancy P., Garcia-Dominguez M., Forchhammer K., Florencio F., Vasudevan S.G., Tandeau de Marsac N., Ollis D.L.
Acta Crystallogr. D 59:2183-2190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62447 Genomic DNA. Translation: AAA27312.1.
CP000100 Genomic DNA. Translation: ABB56353.1.
PIRA39696.
RefSeqYP_399340.1. NC_007604.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QY7X-ray2.00A/B/C1-112[»]
2JJ4X-ray3.46D/E/F1-112[»]
2V5HX-ray2.75G/H/I/J/K/L1-112[»]
2XBPX-ray1.20A1-112[»]
2XG8X-ray3.20A/B/C1-112[»]
2XULX-ray2.20A/B/C/D/E/F1-112[»]
2XZWX-ray1.95A/B/C/D/E/F/G/H/I1-112[»]
4AFFX-ray1.05A1-112[»]
ProteinModelPortalP0A3F4.
SMRP0A3F4. Positions 1-111.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35002N.
IntActP0A3F4. 8 interactions.
STRING1140.Synpcc7942_0321.

PTM databases

PhosSiteP010479.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB56353; ABB56353; Synpcc7942_0321.
GeneID3774842.
KEGGsyf:Synpcc7942_0321.
PATRIC23785713. VBISynElo51371_0401.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0347.
HOGENOMHOG000017847.
KOK04751.
ProtClustDBCLSK895726.

Enzyme and pathway databases

BioCycSELO1140:GJWQ-327-MONOMER.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
InterProIPR002187. N-reg_PII.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
IPR017918. N-reg_PII_CS.
IPR002332. N-reg_PII_urydylation_site.
[Graphical view]
PfamPF00543. P-II. 1 hit.
[Graphical view]
PRINTSPR00340. PIIGLNB.
SMARTSM00938. P-II. 1 hit.
[Graphical view]
SUPFAMSSF54913. N-reg_PII-like_a/b. 1 hit.
PROSITEPS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A3F4.

Entry information

Entry nameGLNB_SYNE7
AccessionPrimary (citable) accession number: P0A3F4
Secondary accession number(s): P80016, Q31RG6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families