Hsp70 family chaperone Hsc62; Probable chaperone. Has ATPase activity. Not stimulated by DnaJ.

DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU; Belongs to the heat shock protein 70 family.

Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity.

Uncharacterized protein; To E.coli YbeU.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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 t [...]

Sel1 family TPR-like repeat protein.

Putative flagella assembly protein; Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering to flip the flagellar T3S specificity switch from the rod and hook-type substrates to filament-type substrates prior to hook-basal body (HBB) completion possibly by preventing interaction of FliK with FlhB (By similarity).

alanyl-tRNA synthetase; Catalyzes the attachment of L-alanine to tRNA(Ala) in a two- step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser. These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step. Attaches Ala to transfer-me [...]