Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N utilization substance protein B

Gene

nusB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

One of the proteins essential for the formation of the RNA polymerase antitermination complex in the presence of lambda phage N protein. However, it is involved in the transcription termination process at certain sites during normal bacterial growth. Binds to the BoxA RNA motif.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10666-MONOMER.
ECOL316407:JW0406-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N utilization substance protein B
Short name:
Protein NusB
Gene namesi
Name:nusB
Synonyms:ssyB
Ordered Locus Names:b0416, JW0406
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10666. nusB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139N utilization substance protein BPRO_0000176536Add
BLAST

Proteomic databases

EPDiP0A780.
PaxDbiP0A780.
PRIDEiP0A780.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsJP0A7R55EBI-555387,EBI-544602

Protein-protein interaction databases

BioGridi4259834. 29 interactions.
DIPiDIP-48254N.
IntActiP0A780. 12 interactions.
MINTiMINT-1220894.
STRINGi511145.b0416.

Structurei

Secondary structure

1
139
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2320Combined sources
Helixi27 – 3711Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 5713Combined sources
Helixi59 – 668Combined sources
Helixi67 – 704Combined sources
Helixi74 – 763Combined sources
Helixi79 – 9416Combined sources
Helixi100 – 11415Combined sources
Helixi119 – 13416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EY1NMR-A1-139[»]
3D3BX-ray1.30A1-139[»]
3D3CX-ray2.60A/B/C1-139[»]
3IMQX-ray2.50A/B/C3-139[»]
ProteinModelPortaliP0A780.
SMRiP0A780. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A780.

Family & Domainsi

Sequence similaritiesi

Belongs to the NusB family.Curated

Phylogenomic databases

eggNOGiENOG4107YIM. Bacteria.
COG0781. LUCA.
HOGENOMiHOG000281868.
InParanoidiP0A780.
KOiK03625.
OMAiWIGVYEF.
OrthoDBiEOG6RJV9B.
PhylomeDBiP0A780.

Family and domain databases

Gene3Di1.10.940.10. 1 hit.
HAMAPiMF_00073. NusB.
InterProiIPR011605. NusB_fam.
IPR006027. NusB_RsmB_TIM44.
[Graphical view]
PANTHERiPTHR11078. PTHR11078. 1 hit.
PfamiPF01029. NusB. 1 hit.
[Graphical view]
SUPFAMiSSF48013. SSF48013. 1 hit.
TIGRFAMsiTIGR01951. nusB. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPAARRRAR ECAVQALYSW QLSQNDIADV EYQFLAEQDV KDVDVLYFRE
60 70 80 90 100
LLAGVATNTA YLDGLMKPYL SRLLEELGQV EKAVLRIALY ELSKRSDVPY
110 120 130
KVAINEAIEL AKSFGAEDSH KFVNGVLDKA APVIRPNKK
Length:139
Mass (Da):15,689
Last modified:June 7, 2005 - v1
Checksum:i0BB912103061243B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591T → S (PubMed:6330693).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181Y → D in nusB5; abolishes antitermination.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00681 Genomic DNA. Translation: CAA25289.1.
X64395 Genomic DNA. Translation: CAA45737.1.
M26839 Genomic DNA. Translation: AAA24228.1.
U82664 Genomic DNA. Translation: AAB40172.1.
U00096 Genomic DNA. Translation: AAC73519.1.
AP009048 Genomic DNA. Translation: BAE76196.1.
PIRiI51822. FJECB.
RefSeqiNP_414950.1. NC_000913.3.
WP_000801125.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73519; AAC73519; b0416.
BAE76196; BAE76196; BAE76196.
GeneIDi945054.
KEGGiecj:JW0406.
eco:b0416.
PATRICi32115981. VBIEscCol129921_0432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00681 Genomic DNA. Translation: CAA25289.1.
X64395 Genomic DNA. Translation: CAA45737.1.
M26839 Genomic DNA. Translation: AAA24228.1.
U82664 Genomic DNA. Translation: AAB40172.1.
U00096 Genomic DNA. Translation: AAC73519.1.
AP009048 Genomic DNA. Translation: BAE76196.1.
PIRiI51822. FJECB.
RefSeqiNP_414950.1. NC_000913.3.
WP_000801125.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EY1NMR-A1-139[»]
3D3BX-ray1.30A1-139[»]
3D3CX-ray2.60A/B/C1-139[»]
3IMQX-ray2.50A/B/C3-139[»]
ProteinModelPortaliP0A780.
SMRiP0A780. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259834. 29 interactions.
DIPiDIP-48254N.
IntActiP0A780. 12 interactions.
MINTiMINT-1220894.
STRINGi511145.b0416.

Proteomic databases

EPDiP0A780.
PaxDbiP0A780.
PRIDEiP0A780.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73519; AAC73519; b0416.
BAE76196; BAE76196; BAE76196.
GeneIDi945054.
KEGGiecj:JW0406.
eco:b0416.
PATRICi32115981. VBIEscCol129921_0432.

Organism-specific databases

EchoBASEiEB0660.
EcoGeneiEG10666. nusB.

Phylogenomic databases

eggNOGiENOG4107YIM. Bacteria.
COG0781. LUCA.
HOGENOMiHOG000281868.
InParanoidiP0A780.
KOiK03625.
OMAiWIGVYEF.
OrthoDBiEOG6RJV9B.
PhylomeDBiP0A780.

Enzyme and pathway databases

BioCyciEcoCyc:EG10666-MONOMER.
ECOL316407:JW0406-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A780.
PROiP0A780.

Family and domain databases

Gene3Di1.10.940.10. 1 hit.
HAMAPiMF_00073. NusB.
InterProiIPR011605. NusB_fam.
IPR006027. NusB_RsmB_TIM44.
[Graphical view]
PANTHERiPTHR11078. PTHR11078. 1 hit.
PfamiPF01029. NusB. 1 hit.
[Graphical view]
SUPFAMiSSF48013. SSF48013. 1 hit.
TIGRFAMsiTIGR01951. nusB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the Escherichia coli K12 nusB (groNB) gene."
    Swindle J., Ajioka J., Dawson D., Myers R., Carroll D., Georgopoulos C.
    Nucleic Acids Res. 12:4977-4985(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and nucleotide sequencing of the nusB gene of E. coli."
    Ishii S., Hatada E., Maekawa T., Imamoto F.
    Nucleic Acids Res. 12:4987-4995(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Escherichia coli proteins involved in regulation of transcription termination: function, structure, and expression of the nusA and nusB genes."
    Imamoto F., Nakamura Y.
    Adv. Biophys. 21:175-192(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation."
    Taura T., Ueguchi C., Shiba K., Ito K.
    Mol. Gen. Genet. 234:429-432(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  5. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "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.
  9. "Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein."
    Huenges M., Rolz C., Gschwind R., Peteranderl R., Berglechner F., Richter G., Bacher A., Kessler H., Gemmecker G.
    EMBO J. 17:4092-4100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "The structure of the transcriptional antiterminator NusB from Escherichia coli."
    Altieri A.S., Mazzulla M.J., Horita D.A., Coats R.H., Wingfield P.T., Das A., Court D.L., Byrd R.A.
    Nat. Struct. Biol. 7:470-474(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiNUSB_ECOLI
AccessioniPrimary (citable) accession number: P0A780
Secondary accession number(s): P04381, Q2MC10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: June 7, 2005
Last modified: March 16, 2016
This is version 97 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.