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Protein

Transcription termination/antitermination protein NusG

Gene

nusG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNA polymerase (RNAP), probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA and phage lambda N-mediated transcriptional antitermination.UniRule annotation9 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription antitermination, Transcription regulation, Transcription termination

Enzyme and pathway databases

BioCyciEcoCyc:EG10667-MONOMER.
ECOL316407:JW3945-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription termination/antitermination protein NusGUniRule annotation
Gene namesi
Name:nusGUniRule annotation
Ordered Locus Names:b3982, JW3945
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10667. nusG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 181180Transcription termination/antitermination protein NusGPRO_0000113926Add
BLAST

Proteomic databases

EPDiP0AFG0.
PaxDbiP0AFG0.
PRIDEiP0AFG0.

2D gel databases

SWISS-2DPAGEP0AFG0.

Interactioni

Subunit structurei

Monomer. Interacts with the transcription termination factor Rho and with RNA polymerase. One NusG monomer forms a stable complex with a Rho hexamer. Binds directly, but weakly, to the core enzyme of RNAP. Also interacts with RpsJ (NusE).UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
crpP0ACJ82EBI-369628,EBI-547513
rhoP0AG306EBI-369628,EBI-545468

Protein-protein interaction databases

BioGridi4259510. 11 interactions.
DIPiDIP-31860N.
IntActiP0AFG0. 54 interactions.
MINTiMINT-1218205.
STRINGi511145.b3982.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Helixi19 – 3315Combined sources
Turni36 – 383Combined sources
Beta strandi68 – 736Combined sources
Helixi77 – 859Combined sources
Beta strandi86 – 9914Combined sources
Helixi105 – 11612Combined sources
Beta strandi132 – 1365Combined sources
Turni140 – 1434Combined sources
Beta strandi144 – 1529Combined sources
Turni153 – 1564Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi167 – 1737Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVVNMR-A1-181[»]
2K06NMR-A1-123[»]
2KVQNMR-G123-181[»]
ProteinModelPortaliP0AFG0.
SMRiP0AFG0. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini130 – 16132KOWUniRule annotationAdd
BLAST

Domaini

The N-terminal domain interacts with RNAP and the C-terminal domain binds either to Rho or to RpsJ (NusE). These domains are separated by a flexible linker.1 Publication

Sequence similaritiesi

Belongs to the NusG family.UniRule annotation
Contains 1 KOW domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E5V. Bacteria.
COG0250. LUCA.
HOGENOMiHOG000219264.
InParanoidiP0AFG0.
KOiK02601.
OMAiAVHTYVG.
OrthoDBiEOG6FFS95.
PhylomeDBiP0AFG0.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
3.30.70.940. 1 hit.
HAMAPiMF_00948. NusG.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR001062. Transcrpt_antiterm_NusG.
IPR015869. Transcrpt_antiterm_NusG_bac_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 1 hit.
PF02357. NusG. 1 hit.
[Graphical view]
PRINTSiPR00338. NUSGTNSCPFCT.
SMARTiSM00739. KOW. 1 hit.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF82679. SSF82679. 1 hit.
TIGRFAMsiTIGR00922. nusG. 1 hit.
PROSITEiPS01014. NUSG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEAPKKRWY VVQAFSGFEG RVATSLREHI KLHNMEDLFG EVMVPTEEVV
60 70 80 90 100
EIRGGQRRKS ERKFFPGYVL VQMVMNDASW HLVRSVPRVM GFIGGTSDRP
110 120 130 140 150
APISDKEVDA IMNRLQQVGD KPRPKTLFEP GEMVRVNDGP FADFNGVVEE
160 170 180
VDYEKSRLKV SVSIFGRATP VELDFSQVEK A
Length:181
Mass (Da):20,532
Last modified:January 23, 2007 - v2
Checksum:iB3AF94284CC17B04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30610 Genomic DNA. Translation: AAA24622.1.
U00006 Genomic DNA. Translation: AAC43080.1.
U00096 Genomic DNA. Translation: AAC76956.1.
AP009048 Genomic DNA. Translation: BAE77338.1.
PIRiB35139. TWECNG.
RefSeqiNP_418409.1. NC_000913.3.
WP_001287516.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76956; AAC76956; b3982.
BAE77338; BAE77338; BAE77338.
GeneIDi948485.
KEGGiecj:JW3945.
eco:b3982.
PATRICi32123485. VBIEscCol129921_4095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30610 Genomic DNA. Translation: AAA24622.1.
U00006 Genomic DNA. Translation: AAC43080.1.
U00096 Genomic DNA. Translation: AAC76956.1.
AP009048 Genomic DNA. Translation: BAE77338.1.
PIRiB35139. TWECNG.
RefSeqiNP_418409.1. NC_000913.3.
WP_001287516.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVVNMR-A1-181[»]
2K06NMR-A1-123[»]
2KVQNMR-G123-181[»]
ProteinModelPortaliP0AFG0.
SMRiP0AFG0. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259510. 11 interactions.
DIPiDIP-31860N.
IntActiP0AFG0. 54 interactions.
MINTiMINT-1218205.
STRINGi511145.b3982.

2D gel databases

SWISS-2DPAGEP0AFG0.

Proteomic databases

EPDiP0AFG0.
PaxDbiP0AFG0.
PRIDEiP0AFG0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76956; AAC76956; b3982.
BAE77338; BAE77338; BAE77338.
GeneIDi948485.
KEGGiecj:JW3945.
eco:b3982.
PATRICi32123485. VBIEscCol129921_4095.

Organism-specific databases

EchoBASEiEB0661.
EcoGeneiEG10667. nusG.

Phylogenomic databases

eggNOGiENOG4105E5V. Bacteria.
COG0250. LUCA.
HOGENOMiHOG000219264.
InParanoidiP0AFG0.
KOiK02601.
OMAiAVHTYVG.
OrthoDBiEOG6FFS95.
PhylomeDBiP0AFG0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10667-MONOMER.
ECOL316407:JW3945-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFG0.
PROiP0AFG0.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
3.30.70.940. 1 hit.
HAMAPiMF_00948. NusG.
InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR014722. Rib_L2_dom2.
IPR001062. Transcrpt_antiterm_NusG.
IPR015869. Transcrpt_antiterm_NusG_bac_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 1 hit.
PF02357. NusG. 1 hit.
[Graphical view]
PRINTSiPR00338. NUSGTNSCPFCT.
SMARTiSM00739. KOW. 1 hit.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF82679. SSF82679. 1 hit.
TIGRFAMsiTIGR00922. nusG. 1 hit.
PROSITEiPS01014. NUSG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
    Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
    J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda."
    Li J., Horwitz R., McCracken S., Greenblatt J.
    J. Biol. Chem. 267:6012-6019(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-12, FUNCTION, INTERACTION WITH RNA POLYMERASE AND RHO FACTOR.
  7. "Requirement for E. coli NusG protein in factor-dependent transcription termination."
    Sullivan S.L., Gottesman M.E.
    Cell 68:989-994(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling."
    Nehrke K.W., Zalatan F., Platt T.
    Gene Expr. 3:119-133(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription."
    Li J., Mason S.W., Greenblatt J.
    Genes Dev. 7:161-172(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHO FACTOR.
  10. "Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro."
    Burova E., Hung S.C., Sagitov V., Stitt B.L., Gottesman M.E.
    J. Bacteriol. 177:1388-1392(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "NusG is required to overcome a kinetic limitation to Rho function at an intragenic terminator."
    Burns C.M., Richardson J.P.
    Proc. Natl. Acad. Sci. U.S.A. 92:4738-4742(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Antiterminator-dependent modulation of transcription elongation rates by NusB and NusG."
    Zellars M., Squires C.L.
    Mol. Microbiol. 32:1296-1304(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex."
    Pasman Z., von Hippel P.H.
    Biochemistry 39:5573-5585(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH RHO.
  14. "In vivo effect of NusB and NusG on rRNA transcription antitermination."
    Torres M., Balada J.M., Zellars M., Squires C., Squires C.L.
    J. Bacteriol. 186:1304-1310(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RRNA TRANSCRIPTION ANTITERMINATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. Cited for: STRUCTURE BY NMR OF 123-181, INTERACTION WITH RPSJ, DOMAIN.

Entry informationi

Entry nameiNUSG_ECOLI
AccessioniPrimary (citable) accession number: P0AFG0
Secondary accession number(s): P16921, Q2M8R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.