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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

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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001397941 – 112Nitrogen regulatory protein P-IIAdd BLAST112

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49Phosphoserine1 Publication1
Modified residuei51O-UMP-tyrosinePROSITE-ProRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP0A3F4.

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.

Protein-protein interaction databases

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

Structurei

Secondary structure

1112
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi10 – 12Combined sources3
Helixi13 – 22Combined sources10
Beta strandi29 – 35Combined sources7
Turni38 – 41Combined sources4
Beta strandi44 – 46Combined sources3
Beta strandi49 – 53Combined sources5
Beta strandi56 – 65Combined sources10
Helixi67 – 69Combined sources3
Helixi70 – 81Combined sources12
Beta strandi84 – 86Combined sources3
Beta strandi89 – 95Combined sources7
Beta strandi98 – 101Combined sources4
Turni102 – 104Combined sources3
Helixi109 – 112Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OrthoDBiPOG091H03RA.

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)DescriptionActionsGraphical viewLength
Sequence conflicti83T → P in AAA27312 (PubMed:1905010).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP0A3F4.

Proteomic databases

PRIDEiP0A3F4.

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.
OrthoDBiPOG091H03RA.

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...

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: November 2, 2016
This is version 92 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.