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Protein

Nitrogen regulatory protein P-II

Gene

glnB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • enzyme regulator activity Source: InterPro
  • identical protein binding Source: IntAct
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_0321-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen regulatory protein P-II
Alternative name(s):
PII signal transducing protein
Gene namesi
Name:glnB
Ordered Locus Names:Synpcc7942_0321
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Nitrogen regulatory protein P-IIPRO_0000139794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei51 – 511O-UMP-tyrosinePROSITE-ProRule annotation

Post-translational modificationi

Phosphorylation dependent on the nitrogen source and spectral light quality.2 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP0A3F4.

Interactioni

Subunit structurei

Homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-700889,EBI-700889
argBQ6V1L56EBI-700889,EBI-700898
tlr2243Q8DGS18EBI-700889,EBI-7629960From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-35002N.
IntActiP0A3F4. 9 interactions.
MINTiMINT-8300504.
STRINGi1140.Synpcc7942_0321.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi10 – 123Combined sources
Helixi13 – 2210Combined sources
Beta strandi29 – 357Combined sources
Turni38 – 414Combined sources
Beta strandi44 – 463Combined sources
Beta strandi49 – 535Combined sources
Beta strandi56 – 6510Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8112Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 957Combined sources
Beta strandi98 – 1014Combined sources
Turni102 – 1043Combined sources
Helixi109 – 1124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4C3KX-ray3.10A/B/C/D/E/F1-112[»]
4C3LX-ray1.60A1-112[»]
4C3MX-ray2.15A/B/C1-112[»]
ProteinModelPortaliP0A3F4.
SMRiP0A3F4. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A3F4.

Family & Domainsi

Sequence similaritiesi

Belongs to the P(II) protein family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108YZA. Bacteria.
COG0347. LUCA.
HOGENOMiHOG000017847.
KOiK04751.
OrthoDBiEOG69GZGV.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
InterProiIPR002187. 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]
PfamiPF00543. P-II. 1 hit.
[Graphical view]
PIRSFiPIRSF039144. GlnB. 1 hit.
PRINTSiPR00340. PIIGLNB.
SMARTiSM00938. P-II. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
PROSITEiPS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A3F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE
60 70 80 90 100
YTVEFLQKLK LEIVVEDAQV DTVIDKIVAA ARTGEIGDGK IFVSPVDQTI
110
RIRTGEKNAD AI
Length:112
Mass (Da):12,391
Last modified:March 15, 2005 - v1
Checksum:i5F44B64CBFF3C559
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831T → P in AAA27312 (PubMed:1905010).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62447 Genomic DNA. Translation: AAA27312.1.
CP000100 Genomic DNA. Translation: ABB56353.1.
PIRiA39696.
RefSeqiWP_011243504.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB56353; ABB56353; Synpcc7942_0321.
KEGGisyf:Synpcc7942_0321.
PATRICi23785713. VBISynElo51371_0401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62447 Genomic DNA. Translation: AAA27312.1.
CP000100 Genomic DNA. Translation: ABB56353.1.
PIRiA39696.
RefSeqiWP_011243504.1. NC_007604.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4C3KX-ray3.10A/B/C/D/E/F1-112[»]
4C3LX-ray1.60A1-112[»]
4C3MX-ray2.15A/B/C1-112[»]
ProteinModelPortaliP0A3F4.
SMRiP0A3F4. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35002N.
IntActiP0A3F4. 9 interactions.
MINTiMINT-8300504.
STRINGi1140.Synpcc7942_0321.

PTM databases

iPTMnetiP0A3F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB56353; ABB56353; Synpcc7942_0321.
KEGGisyf:Synpcc7942_0321.
PATRICi23785713. VBISynElo51371_0401.

Phylogenomic databases

eggNOGiENOG4108YZA. Bacteria.
COG0347. LUCA.
HOGENOMiHOG000017847.
KOiK04751.
OrthoDBiEOG69GZGV.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_0321-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A3F4.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
InterProiIPR002187. 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]
PfamiPF00543. P-II. 1 hit.
[Graphical view]
PIRSFiPIRSF039144. GlnB. 1 hit.
PRINTSiPR00340. PIIGLNB.
SMARTiSM00938. P-II. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
PROSITEiPS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiGLNB_SYNE7
AccessioniPrimary (citable) accession number: P0A3F4
Secondary accession number(s): P80016, Q31RG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 20, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.