Q55247 (GLNB_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nitrogen regulatory protein P-II Alternative name(s): PII signal transducing protein | ||||
| Gene names |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 112 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 By similarity. |
| Subunit structure | Homotrimer By similarity. |
| Post-translational modification | Phosphorylation dependent on the nitrogen source and spectral light quality By similarity. |
| Sequence similarities | Belongs to the P(II) protein family. |
| Sequence caution | The sequence BAA18533.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Ligand | Nucleotide-binding |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | regulation of catalytic activity Inferred from electronic annotation. Source: GOC regulation of nitrogen utilizationInferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | enzyme regulator activity Inferred from electronic annotation. Source: InterPro nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| sll0985 | P73148 | 5 | EBI-906365,EBI-906297 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 112 | 112 | Nitrogen regulatory protein P-II | PRO_0000139795 | |||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||
| Modified residue | 49 | 1 | Phosphoserine Probable | ||||||||||||||||||||||||||
| Modified residue | 51 | 1 | O-UMP-tyrosine By similarity | ||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||
| Beta strand | 2 – 8 | 7 | |||||||||||||||||||||||||||
| Helix | 10 – 12 | 3 | |||||||||||||||||||||||||||
| Helix | 13 – 21 | 9 | |||||||||||||||||||||||||||
| Turn | 22 – 24 | 3 | |||||||||||||||||||||||||||
| Beta strand | 28 – 35 | 8 | |||||||||||||||||||||||||||
| Beta strand | 56 – 65 | 10 | |||||||||||||||||||||||||||
| Helix | 67 – 69 | 3 | |||||||||||||||||||||||||||
| Helix | 70 – 81 | 12 | |||||||||||||||||||||||||||
| Beta strand | 90 – 95 | 6 | |||||||||||||||||||||||||||
| Beta strand | 98 – 101 | 4 | |||||||||||||||||||||||||||
| Turn | 102 – 104 | 3 | |||||||||||||||||||||||||||
| Beta strand | 107 – 109 | 3 | |||||||||||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Nitrogen availability and electron transport control the expression of glnB gene (encoding PII protein) in the cyanobacterium Synechocystis sp. PCC 6803." Garcia-Dominguez M., Florencio F.J. Plant Mol. Biol. 35:723-734(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
| [3] | "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). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X97496 Genomic DNA. Translation: CAA66127.1. BA000022 Genomic DNA. Translation: BAA18533.1. Different initiation. | ||||||||||||
| PIR | S76404. | ||||||||||||
| RefSeq | NP_441855.2. NC_000911.1. YP_005651915.1. NC_017277.1. YP_007451736.1. NC_020286.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q55247. | ||||||||||||
| SMR | Q55247. Positions 1-112. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q55247. 3 interactions. | ||||||||||||
| STRING | 1148.ssl0707. | ||||||||||||
PTM databases | |||||||||||||
| PhosSite | P0806321. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q55247. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | BAA18533; BAA18533; BAA18533. | ||||||||||||
| GeneID | 12254574. 14617403. 952897. | ||||||||||||
| KEGG | syn:ssl0707. syy:SYNGTS_1962. | ||||||||||||
| PATRIC | 23841230. VBISynSp132158_2165. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0347. | ||||||||||||
| HOGENOM | HOG000017847. | ||||||||||||
| KO | K04751. | ||||||||||||
| OMA | GFIAMTI. | ||||||||||||
| ProtClustDB | CLSK895726. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.30.70.120. 1 hit. | ||||||||||||
| InterPro | IPR002187. 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] | ||||||||||||
| Pfam | PF00543. P-II. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00340. PIIGLNB. | ||||||||||||
| SMART | SM00938. P-II. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF54913. N-reg_PII-like_a/b. 1 hit. | ||||||||||||
| PROSITE | PS00638. PII_GLNB_CTER. 1 hit. PS51343. PII_GLNB_DOM. 1 hit. PS00496. PII_GLNB_UMP. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q55247. | ||||||||||||
Entry information
| Entry name | GLNB_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55247 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
