UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.

Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.

Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]

PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; KEGG: tcx:Tcr_0779 DEAD/DEAH box helicase-like; Belongs to the DEAD box helicase family.

ATP-dependent RNA helicase CsdA; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.

PFAM: ribosomal protein L27; KEGG: vch:VC0436 50S ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family.

3-oxoacyl-[acyl-carrier-protein] reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family.

SSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.

Translation elongation factor 2 (EF-2/EF-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. [...]