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Protein

Nitrogen regulatory protein P-II 1

Gene

glnB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

P-II indirectly controls the transcription of the glutamine synthetase 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 uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.

GO - Molecular functioni

  • ATP binding Source: EcoCyc
  • enzyme regulator activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • small molecule binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PROTEIN-PII.
ECOL316407:JW2537-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen regulatory protein P-II 1
Gene namesi
Name:glnB
Ordered Locus Names:b2553, JW2537
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10384. glnB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Nitrogen regulatory protein P-II 1PRO_0000139771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511O-UMP-tyrosinePROSITE-ProRule annotation1 Publication

Post-translational modificationi

Uridylylated/deuridylylated by GlnD.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP0A9Z1.
PaxDbiP0A9Z1.
PRIDEiP0A9Z1.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-551053,EBI-551053
glnDP272493EBI-551053,EBI-552032
glnKP0AC553EBI-551053,EBI-559503
glnLP0AFB55EBI-551053,EBI-701156
rraBP0AF902EBI-551053,EBI-544031

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259201. 28 interactions.
DIPiDIP-35005N.
IntActiP0A9Z1. 18 interactions.
MINTiMINT-1235669.
STRINGi511145.b2553.

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 – 2311Combined sources
Beta strandi29 – 357Combined sources
Beta strandi50 – 523Combined sources
Beta strandi56 – 6510Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8112Combined sources
Beta strandi91 – 955Combined sources
Turni102 – 1043Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PILX-ray2.70A1-112[»]
2PIIX-ray1.90A1-112[»]
ProteinModelPortaliP0A9Z1.
SMRiP0A9Z1. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9Z1.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0347. LUCA.
HOGENOMiHOG000017847.
InParanoidiP0A9Z1.
KOiK04751.
OMAiAIEVKGF.
OrthoDBiEOG69GZGV.
PhylomeDBiP0A9Z1.

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.

P0A9Z1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIDAIIKP FKLDDVREAL AEVGITGMTV TEVKGFGRQK GHTELYRGAE
60 70 80 90 100
YMVDFLPKVK IEIVVPDDIV DTCVDTIIRT AQTGKIGDGK IFVFDVARVI
110
RIRTGEEDDA AI
Length:112
Mass (Da):12,425
Last modified:September 13, 2005 - v1
Checksum:iD1A4158A2F225042
GO

Sequence cautioni

The sequence AAA23883.1 differs from that shown. Reason: Frameshift at positions 103 and 105. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191A → R in AAA23883 (PubMed:2885322).Curated
Sequence conflicti81 – 822AQ → E in AAA23883 (PubMed:2885322).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16778 Genomic DNA. Translation: AAA23883.1. Frameshift.
X58872 Genomic DNA. Translation: CAA41683.1.
S67014 Genomic DNA. Translation: AAB28779.1.
U00096 Genomic DNA. Translation: AAC75606.1.
AP009048 Genomic DNA. Translation: BAA16461.1.
Z21843 Genomic DNA. Translation: CAA79890.1.
PIRiC49940. RGECP2.
RefSeqiNP_417048.1. NC_000913.3.
WP_000717694.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75606; AAC75606; b2553.
BAA16461; BAA16461; BAA16461.
GeneIDi23339395.
947016.
KEGGiecj:JW2537.
eco:b2553.
PATRICi32120505. VBIEscCol129921_2655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16778 Genomic DNA. Translation: AAA23883.1. Frameshift.
X58872 Genomic DNA. Translation: CAA41683.1.
S67014 Genomic DNA. Translation: AAB28779.1.
U00096 Genomic DNA. Translation: AAC75606.1.
AP009048 Genomic DNA. Translation: BAA16461.1.
Z21843 Genomic DNA. Translation: CAA79890.1.
PIRiC49940. RGECP2.
RefSeqiNP_417048.1. NC_000913.3.
WP_000717694.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PILX-ray2.70A1-112[»]
2PIIX-ray1.90A1-112[»]
ProteinModelPortaliP0A9Z1.
SMRiP0A9Z1. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259201. 28 interactions.
DIPiDIP-35005N.
IntActiP0A9Z1. 18 interactions.
MINTiMINT-1235669.
STRINGi511145.b2553.

Proteomic databases

EPDiP0A9Z1.
PaxDbiP0A9Z1.
PRIDEiP0A9Z1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75606; AAC75606; b2553.
BAA16461; BAA16461; BAA16461.
GeneIDi23339395.
947016.
KEGGiecj:JW2537.
eco:b2553.
PATRICi32120505. VBIEscCol129921_2655.

Organism-specific databases

EchoBASEiEB0379.
EcoGeneiEG10384. glnB.

Phylogenomic databases

eggNOGiCOG0347. LUCA.
HOGENOMiHOG000017847.
InParanoidiP0A9Z1.
KOiK04751.
OMAiAIEVKGF.
OrthoDBiEOG69GZGV.
PhylomeDBiP0A9Z1.

Enzyme and pathway databases

BioCyciEcoCyc:PROTEIN-PII.
ECOL316407:JW2537-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9Z1.
PROiP0A9Z1.

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. "Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene."
    Son H.S., Rhee S.G.
    J. Biol. Chem. 262:8690-8695(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], URIDYLYLATION AT TYR-51.
  2. "Identification of the Klebsiella pneumoniae glnB gene: nucleotide sequence of wild-type and mutant alleles."
    Holtel A., Merrick M.
    Mol. Gen. Genet. 215:134-138(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12."
    Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., Poole R.K.
    Mol. Gen. Genet. 226:49-58(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "The glnB region of the Escherichia coli chromosome."
    Liu J., Magasanik B.
    J. Bacteriol. 175:7441-7449(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
    van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
    Mol. Microbiol. 9:443-458(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Regulation of transcription of the glnALG operon of Escherichia coli by protein phosphorylation."
    Magasanik B.
    Biochimie 71:1005-1012(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Escherichia coli PII protein: purification, crystallization and oligomeric structure."
    Vasudevan S.G., Gedye C., Dixon N.E., Cheah E., Carr P.D., Suffolk P.M., Jeffrey P.D., Ollis D.L.
    FEBS Lett. 337:255-258(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "Structure of the Escherichia coli signal transducing protein PII."
    Cheah E., Carr P.D., Suffolk P.M., Vasuvedan S.G., Dixon N.E., Ollis D.L.
    Structure 2:981-990(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  13. "X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A."
    Carr P.D., Cheah E., Suffolk P.M., Vasudevan S.G., Dixon N.E., Ollis D.L.
    Acta Crystallogr. D 52:93-104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiGLNB_ECOLI
AccessioniPrimary (citable) accession number: P0A9Z1
Secondary accession number(s): P05826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: March 16, 2016
This is version 95 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.