DSBA-like thioredoxin domain protein; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily.

TPR repeat family protein.

Organic solvent tolerance family protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.

flgF: flagellar basal-body rod protein FlgF; Belongs to the flagella basal body rod proteins family.

Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Tetratricopeptide repeat family protein.

cobD/Cbib family protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.

Twin arginine-targeting protein translocase TatB; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.

protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.