RpoE
- Description: RNA polymerase delta subunit
Gene name | rpoE |
Synonyms | |
Essential | no |
Product | RNA polymerase delta subunit |
Function | transcription |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 20 kDa, 3.654 |
Gene length, protein length | 519 bp, 173 aa |
Immediate neighbours | pyrG, acdA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU37160
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: rpoE family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions: closely associated to RNA polymerase (RpoA(2)-RpoB-RpoC) PubMed
- Localization:closely associated with RNA polymerase involved in transcribing both mRNA and rRNA operons PubMed
Database entries
- UniProt: P12464
- KEGG entry: [3]
- E.C. number: 2.7.7.6
Additional information
Expression and regulation
- Additional information:
- present at equimolar levels with RNA polymerase PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
Your additional remarks
References
Geoff P Doherty, Mark J Fogg, Anthony J Wilkinson, Peter J Lewis
Small subunits of RNA polymerase: localization, levels and implications for core enzyme composition.
Microbiology (Reading): 2010, 156(Pt 12);3532-3543
[PubMed:20724389]
[WorldCat.org]
[DOI]
(I p)
Veronika Motácková, Hana Sanderová, Lukás Zídek, Jirí Novácek, Petr Padrta, Alzbeta Svenková, Jana Korelusová, Jirí Jonák, Libor Krásný, Vladimír Sklenár
Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs.
Proteins: 2010, 78(7);1807-10
[PubMed:20310067]
[WorldCat.org]
[DOI]
(I p)
Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250]
[WorldCat.org]
[DOI]
(P p)
F J López de Saro, N Yoshikawa, J D Helmann
Expression, abundance, and RNA polymerase binding properties of the delta factor of Bacillus subtilis.
J Biol Chem: 1999, 274(22);15953-8
[PubMed:10336502]
[WorldCat.org]
[DOI]
(P p)
F J López de Saro, A Y Woody, J D Helmann
Structural analysis of the Bacillus subtilis delta factor: a protein polyanion which displaces RNA from RNA polymerase.
J Mol Biol: 1995, 252(2);189-202
[PubMed:7545758]
[WorldCat.org]
[DOI]
(P p)
Y L Juang, J D Helmann
Pathway of promoter melting by Bacillus subtilis RNA polymerase at a stable RNA promoter: effects of temperature, delta protein, and sigma factor mutations.
Biochemistry: 1995, 34(26);8465-73
[PubMed:7599136]
[WorldCat.org]
[DOI]
(P p)
Y L Juang, J D Helmann
The delta subunit of Bacillus subtilis RNA polymerase. An allosteric effector of the initiation and core-recycling phases of transcription.
J Mol Biol: 1994, 239(1);1-14
[PubMed:7515111]
[WorldCat.org]
[DOI]
(P p)
M Lampe, C Binnie, R Schmidt, R Losick
Cloned gene encoding the delta subunit of Bacillus subtilis RNA polymerase.
Gene: 1988, 67(1);13-9
[PubMed:2843435]
[WorldCat.org]
[DOI]
(P p)
E I Hyde, M D Hilton, H R Whiteley
Interactions of Bacillus subtilis RNA polymerase with subunits determining the specificity of initiation. Sigma and delta peptides can bind simultaneously to core.
J Biol Chem: 1986, 261(35);16565-70
[PubMed:3097010]
[WorldCat.org]
(P p)
E C Achberger, H R Whiteley
The role of the delta peptide of the Bacillus subtilis RNA polymerase in promoter selection.
J Biol Chem: 1981, 256(14);7424-32
[PubMed:6788769]
[WorldCat.org]
(P p)
Additional publications: PubMed