DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.

DNA gyrase subunit B; Derived by automated computational analysis using gene prediction method: Protein Homology.

TetR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.

Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.

ATP F0F1 synthase subunit delta; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction; Belongs to the ATPase delta chain family.

Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.

Twin-arginine translocation pathway; Derived by automated computational analysis using gene prediction method: Protein Homology.

Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.

Molecular chaperone 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, [...]