Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily.

Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.

Periplasmic thioredoxin of cytochrome c-type biogenesis; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD.

Thiol:disulfide interchange protein, periplasmic; Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro. Belongs to the thioredoxin family. DsbC subfamily.

50S ribosomal protein L16 arginine hydroxylase; Growth-regulating oxygenase that catalyzes the hydroxylation of 50S ribosomal protein L16 on 'Arg-81'.

Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Primosome factor n' (replication factor Y); Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Is also involved in initiation of normal DNA replication in various plasmids and phages. Binds to branched DNA structures that resemble D-loops or to the primosome assembly site (PAS). Binds to DNA in two distinct modes, either dependent on or independent of [...]

Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family.

Putative flagellar basal body protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.