Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]

Ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.

YjeF-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...]

Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.

Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.

Ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.

This gene is aparrently the terminal component of a non-ribosomal peptide synthetase (due to the presence of the terminal thioesterase domain) and is most likely associated with the previous gene which appears to be a initiating component. This gene contains three complete amino acid activation, thiolation and condensation domain modules and appears to be specific for glycine, an unidentified amino acid and serine according to the prediction algorithm at http://raynam.chm.jhu.edu/; nrps/index2.html. Taken together these two genes appear to direct the biosynthesis of a previously undesc [...]

Coronamic acid synthetase CmaA; Non-ribosomal peptide synthetase with adenylation and thiolation domains; reacts with the AMP derivative of L-allo-isoleucine to produce an aminoacyl thiolester intermediate during coronamic acid biosynthesis; see PMID: 14679222; see PMID:20190049 for expression data; non-ribosomal peptide synthetase with adenylation and thiolation domains, reacts with the AMP derivative of L-allo-isoleucine to produce an aminoacyl thiolester intermediate during coronamic acid biosynthesis, see PMID: 14679222.

Conserved protein of unknown function; See PMID:20190049 for expression data; similar to GP:15978392, and GP:15978392; identified by sequence similarity; putative.