Similar to E. coli acrAB operon repressor (AAC73566.1); Blastp hit to AAC73566.1 (215 aa), 87% identity in aa 1 - 214.

Transcriptional regulator (AraC/XylS family) for ara operon; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose.

Similar to E. coli acrAB operon repressor (AAC73566.1); Blastp hit to AAC73566.1 (215 aa), 87% identity in aa 1 - 214.

Transcriptional repressor of marRAB operon; Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.

Similar to E. coli acrAB operon repressor (AAC73566.1); Blastp hit to AAC73566.1 (215 aa), 87% identity in aa 1 - 214.

Redox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity).

Transcriptional regulator (AraC/XylS family) for ara operon; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose.

Similar to E. coli acrAB operon repressor (AAC73566.1); Blastp hit to AAC73566.1 (215 aa), 87% identity in aa 1 - 214.

Transcriptional regulator (AraC/XylS family) for ara operon; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose.

Transcriptional repressor of marRAB operon; Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.

Transcriptional regulator (AraC/XylS family) for ara operon; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose.

Redox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity).

Heat shock protein 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, [...]

Chaperone Hsp70; Acts as a chaperone.

Heat shock protein 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, [...]

Molecular chaparone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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-depe [...]

Heat shock protein 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, [...]

Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat shock protein 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, [...]

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Heat shock protein 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, [...]

Redox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity).

Chaperone Hsp70; Acts as a chaperone.

Heat shock protein 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, [...]

Chaperone Hsp70; Acts as a chaperone.

Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Chaperone Hsp70; Acts as a chaperone.

Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Chaperone Hsp70; Acts as a chaperone.

Molecular chaparone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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-depe [...]

Chaperone Hsp70; Acts as a chaperone.

Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Chaperone Hsp70; Acts as a chaperone.

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Flagellar biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.

Flagellar biosynthesis protein; Cell-proximal portion of basal-body rod; flagellar basal-body rod protein FLGC (putative proximal rod protein). (SW:FLGC_SALTY); Belongs to the flagella basal body rod proteins family.

Flagellar biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.

Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

Flagellar biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.

Filament capping protein; Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end; Belongs to the FliD family.