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Protein

Nitrogen regulatory protein P-II

Gene

glnB

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

  1. enzyme regulator activity Source: InterPro
  2. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of nitrogen utilization Source: InterPro
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Nucleotide-binding

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:ssl0707
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Nitrogen regulatory protein P-IIPRO_0000139795Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylation dependent on the nitrogen source and spectral light quality.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ55247.

PTM databases

PhosSiteiP0806321.

Interactioni

Subunit structurei

Homotrimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
sll0985P731485EBI-906365,EBI-906297

Protein-protein interaction databases

IntActiQ55247. 3 interactions.
STRINGi1148.ssl0707.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi10 – 123Combined sources
Helixi13 – 219Combined sources
Turni22 – 243Combined sources
Beta strandi28 – 358Combined sources
Beta strandi56 – 6510Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8112Combined sources
Beta strandi90 – 956Combined sources
Beta strandi98 – 1014Combined sources
Turni102 – 1043Combined sources
Beta strandi107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UL3X-ray2.00A/B/C/D1-112[»]
ProteinModelPortaliQ55247.
SMRiQ55247. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55247.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0347.
HOGENOMiHOG000017847.
InParanoidiQ55247.
KOiK04751.
OMAiAIEVKGF.
PhylomeDBiQ55247.

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]
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.

Q55247-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKVEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE
60 70 80 90 100
YTVEFLQKLK IEIVVDEGQV DMVVDKLVSA ARTGEIGDGK IFISPVDSVV
110
RIRTGEKDTE AI
Length:112
Mass (Da):12,397
Last modified:November 1, 1997 - v1
Checksum:iF9ABD0F5C173B799
GO

Sequence cautioni

The sequence BAA18533.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97496 Genomic DNA. Translation: CAA66127.1.
BA000022 Genomic DNA. Translation: BAA18533.1. Different initiation.
PIRiS76404.
RefSeqiNP_441855.2. NC_000911.1.
YP_005651915.1. NC_017277.1.
YP_007451736.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA18533; BAA18533; BAA18533.
GeneIDi952897.
KEGGisyn:ssl0707.
PATRICi23841230. VBISynSp132158_2165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97496 Genomic DNA. Translation: CAA66127.1.
BA000022 Genomic DNA. Translation: BAA18533.1. Different initiation.
PIRiS76404.
RefSeqiNP_441855.2. NC_000911.1.
YP_005651915.1. NC_017277.1.
YP_007451736.1. NC_020286.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UL3X-ray2.00A/B/C/D1-112[»]
ProteinModelPortaliQ55247.
SMRiQ55247. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ55247. 3 interactions.
STRINGi1148.ssl0707.

PTM databases

PhosSiteiP0806321.

Proteomic databases

PaxDbiQ55247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA18533; BAA18533; BAA18533.
GeneIDi952897.
KEGGisyn:ssl0707.
PATRICi23841230. VBISynSp132158_2165.

Phylogenomic databases

eggNOGiCOG0347.
HOGENOMiHOG000017847.
InParanoidiQ55247.
KOiK04751.
OMAiAIEVKGF.
PhylomeDBiQ55247.

Miscellaneous databases

EvolutionaryTraceiQ55247.

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]
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. "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.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., 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).

Entry informationi

Entry nameiGLNB_SYNY3
AccessioniPrimary (citable) accession number: Q55247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 102 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3

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 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.