EcoGene

GenePage for the tufB gene of Escherichia coli K-12

APEX: 87672.53

Bacteriome: tufB

ChemGen Gene Correlations: tufB

ChemGen Growth Data: tufB

Gene-Profiles.org: tufB

Genevestigator: P0CE48

GenExpDB: b3980

Genome3D: P0CE48

GenomeReviews: P0CE48

GenPept: NP_418407.1

GenPept-GenBank: AAC76954

MicrobesOnline: P0CE48

ProteinOntology: 000024141

ProteomeFolding at YRC: P0CE48

TF Binding Sites: tufB.html

xbase-ColiBASE: b3980

Primary Gene Name: tufB
EcoGene Accession Number: EG11037
K-12 Gene Accession Number: ECK3971
MG1655 Gene Identifier: b3980

Kinetically Stable Proteins

Oxidized Proteins

Oxidized Proteins, Carbon

Oxidized Proteins, Nitrogen

Protein Lysine Acetylation: Yu, 2008

Translation Factors

Verified Set

Verified Translation Starts (+Met)

Verified Translation Starts Sites

[Pt(dien)(H2O)]2+

Gene Name Mnemonic: Translation unstable factor

Alternate Gene Symbols: kirT, pulT

Description:
EF-Tu, Elongation Factor-Translation, unstable; GTP-dependent binding of aa-tRNA to the A-site of ribosomes; has intrinsic GTPase activity when bound to kirromycin; subunit of RNA phage Q beta replicase

Pre-Run BlastP UniProt

Protein Sequence ------------ MW: 43313.58------394 aa ------------ Pre-Run BlastP NR+Env

Genomic Address
Left End: 4173967 ----------------- Clockwise ----------------- Right End: 4175151
Left Inter Gene Info Minute or Centisome (%) = 89.96 Right Inter Gene Info

PDF EcoMap

Curator or user-submitted Comments:

EF-Tu is the most abundant protein in E. coli comprising 5-10% of total cellular protein, well in excess of translational requirements (Furano, 1975; Jacobson, 1976; Neidhardt, 1977; Miyajima, 1978; Pedersen, 1978; Young, 1981; van der Meide, 1983). The only amino acid difference between TufA and TufB is the last amino acid, G394 in TufA and S394 in TufB. EF-Tu lysines K38, K177, K249, K253, K295 and K314 can be modified to N6-succinyllysine (Zhang, 2011). EF-Tu lysines K177, K188, K209 and K314 can be modified to N6-acetyllysine (Yu, 2008; Zhang, 2009). HipA binds and phosphorylates EF-Tu residue Thr-383 (Schumacher, 2009). EF-Tu can be modified at K57 to either N6-monomethyllysine or N6,N6-dimethyllysine; the methyltransferases responsible for these modifications are unknown (L'Italien, 1979; G.F.-L. Ames, 1979). Methylation of EF-Tu at K57 impedes GTP hydrolysis in vitro (Van Noort, 1986). Nutrient starvation promotes the conversion of N6-monomethlylysine to N6,N6-dimethyllysine at K57 in E. coli B EF-Tu (Young, 1990; Young, 1991). tufA encodes an essential function, with duplicate gene tufB, such that tufA or tufB can be deleted, but the double mutant is inviable. Coliphage Q beta replicase is comprised of the phage-encoded beta subunit and three bacterial proteins: TufB, Tsf and RpsA (Kondo, 1970; Kamen, 1970; Blumenthal, 1972; Wahba, 1974). RpsA is dispensible for RNA synthesis by coliphage Q beta replicase and is not part of the core replicase (Kamen, 1972; Hori, 1974; Landers, 1974). 50-80% of EF-Tu can be located at the cytoplasmic membrane, possibly as a result of nutrient stress, and EF-Tu may have a ribosome-independent role since it is present in at least a four-fold molar excess over ribosomes; methylation status of K57 may be related to membrane localization (Jacobson, 1976; Young, 1991). Various mutants and growth conditions have demonstrated that EF-Tu, or a precursor form pTu, can be localized to the outer membrane (Dombou, 1981; Lifson, 1986; Sedgwick, 1986). EF-Tu can form filamentous structures in vitro and has been suggested to be an actin-like cytoskeletal protein (Minkoff, 1975; Minkoff, 1976; Rosenbusch, 1976; Jacobson, 1976; Minkoff, 1977; Beck, 1978; Wurtz, 1978; Beck, 1979; Cremers, 1981; Schilstra, 1986; Helms, 1995; Helms, 1996; Norris, 2007). Although early results indicated a lack of an in vivo EF-Tu cytoskeletal structure in E. coli, subsequent experiments identified a helically organized EF-Tu-containing intracellular protofilament near the inner face of the cytoplasmic membrane with polysomes attached; it was suggested that an EF-Tu-containing cytoskeletal web might be the original prokaryotic cytoskeleton and that MreB evolved later to build upon the EF-Tu cytoplasmic network and be a cell shape determinant (Schilstra, 1984; Mayer, 2003; Mayer, 2006). In B. subtilis, EF-Tu is found in a static helical structure at the inner face of the cytoplasmic membrane co-localized with MreB; MreB and EF-Tu interact in vivo and in vitro; reduction of intracellular EF-Tu affects cell shape but not translation efficiency; EF-Tu intracellular protofilaments may serve as tracks for dynamic MreB shape-determining filaments (Defeu, 2010).