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Protein

Antitermination protein N

Gene

N

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role as a transcriptional antitermination factor that allows the virus to initiate its lytic phase. Activates expression of the delayed viral early genes by modifying host RNA polymerase (RNAP) into a form that is resistant to termination signals. This antitermination function requires the host NusA protein which serves to stabilize the interaction between antitermination protein N and host RNA polymerase.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Antitermination protein N
Alternative name(s):
Regulatory protein N
Short name:
PN
Gene namesi
Name:N
Ordered Locus Names:lambdap49
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000001711 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Antitermination protein NPRO_0000077583Add
BLAST

Interactioni

Subunit structurei

Interacts with host nusA.1 Publication

Protein-protein interaction databases

IntActiP03045. 7 interactions.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Helixi12 – 209Combined sources
Helixi23 – 253Combined sources
Beta strandi26 – 294Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFQNMR-B2-36[»]
DisProtiDP00005.
ProteinModelPortaliP03045.
SMRiP03045. Positions 2-36.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03045.

Family & Domainsi

Family and domain databases

InterProiIPR020952. Antiterm_prot_N_Arg-rich.
[Graphical view]
PfamiPF11438. N36. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAQTRRRER RAEKQAQWKA ANPLLVGVSA KPVNRPILSL NRKPKSRVES
60 70 80 90 100
ALNPIDLTVL AEYHKQIESN LQRIERKNQR TWYSKPGERG ITCSGRQKIK

GKSIPLI
Length:107
Mass (Da):12,298
Last modified:February 8, 2011 - v3
Checksum:iF1EBAA32F3A1FE21
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351R → L in AAA32249 (PubMed:2821265).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96578.1.
M29653 Genomic DNA. Translation: AAA32249.1.
PIRiD94614. VNBPL.
RefSeqiNP_040625.1. NC_001416.1.

Genome annotation databases

GeneIDi2703540.
KEGGivg:2703540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96578.1.
M29653 Genomic DNA. Translation: AAA32249.1.
PIRiD94614. VNBPL.
RefSeqiNP_040625.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFQNMR-B2-36[»]
DisProtiDP00005.
ProteinModelPortaliP03045.
SMRiP03045. Positions 2-36.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03045. 7 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703540.
KEGGivg:2703540.

Miscellaneous databases

EvolutionaryTraceiP03045.

Family and domain databases

InterProiIPR020952. Antiterm_prot_N_Arg-rich.
[Graphical view]
PfamiPF11438. N36. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Lambda N antitermination system: functional analysis of phage interactions with the host NusA protein."
    Schauer A.T., Carver D.L., Bigelow B., Baron L.S., Friedman D.I.
    J. Mol. Biol. 194:679-690(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The DNA sequence of the phage lambda genome between PL and the gene bet."
    Ineichen K., Shepherd J.C.W., Bickle T.A.
    Nucleic Acids Res. 9:4639-4653(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The N protein of bacteriophage lambda, defined by its DNA sequence, is highly basic."
    Franklin N.C., Bennett G.N.
    Gene 8:107-119(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Functional importance of regions in Escherichia coli elongation factor NusA that interact with RNA polymerase, the bacteriophage lambda N protein and RNA."
    Mah T.F., Li J., Davidson A.R., Greenblatt J.
    Mol. Microbiol. 34:523-537(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST NUSA.
  6. "Transcription termination and anti-termination in E. coli."
    Nudler E., Gottesman M.E.
    Genes Cells 7:755-768(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  7. "Bacteriophage lambda N protein inhibits transcription slippage by Escherichia coli RNA polymerase."
    Parks A.R., Court C., Lubkowska L., Jin D.J., Kashlev M., Court D.L.
    Nucleic Acids Res. 42:5823-5829(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex."
    Scharpf M., Sticht H., Schweimer K., Boehm M., Hoffmann S., Rosch P.
    Eur. J. Biochem. 267:2397-2408(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-34.

Entry informationi

Entry nameiREGN_LAMBD
AccessioniPrimary (citable) accession number: P03045
Secondary accession number(s): Q38647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 8, 2011
Last modified: December 9, 2015
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral 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

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.