Multifunctional: transcriptional repressor of proline utilization; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family.

Thioredoxin reductase, FAD/NAD(P)-binding.

Conserved hypothetical protein.

Hypothetical protein; putative exported protein.

Putative toxin RtxA protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; phenotype.

Protein chain elongation factor EF-G, GTP-binding; 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 f [...]

Cytolysin-activating lysine-acyltransferase rtxC; Function of strongly homologous gene; factor.

Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

ATPase component of the HslUV protease, also functions as molecular chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.