F1 sector of membrane-bound ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane; Belongs to the ATPase epsilon chain family.

F0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.

F1 sector of membrane-bound ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane; Belongs to the ATPase epsilon chain family.

ATP synthase, membrane-bound accessory factor; A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex; Belongs to the bacterial AtpI family.

F0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.

F1 sector of membrane-bound ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane; Belongs to the ATPase epsilon chain family.

F0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.

ATP synthase, membrane-bound accessory factor; A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex; Belongs to the bacterial AtpI family.

ATP synthase, membrane-bound accessory factor; A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex; Belongs to the bacterial AtpI family.

F1 sector of membrane-bound ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane; Belongs to the ATPase epsilon chain family.

ATP synthase, membrane-bound accessory factor; A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex; Belongs to the bacterial AtpI family.

F0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.

Transcriptional regulator of rRNA transcription; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic terminat [...]

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.

Transcriptional regulator of rRNA transcription; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic terminat [...]

PcnB-degradosome interaction factor; Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co- degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. In stationary phase, could also act as an anti-sigma factor and reduce the ability of RpoS to activate gene expression. Is also involved in the regulation of the mRNA polyadenylation pathway during stationary phase, probably by maintaining the asso [...]

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.

Transcriptional regulator of rRNA transcription; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic terminat [...]

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.

16S rRNA m(6)A1518, m(6)A1519 dimethyltransferase, SAM-dependent; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and may play a role in protection of DNA against oxidative stress.

D-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily.

D,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.

D-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily.

ADP-heptose:LPS heptosyl transferase I; Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA; Belongs to the glycosyltransferase 9 family.

D-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily.

UDP-glucose:(heptosyl)lipopolysaccharide alpha-1,3-glucosyltransferase; Involved in the addition of the first glucose residue to the lipopolysaccharide core; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

D-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily.

Kinase that phosphorylates core heptose of lipopolysaccharide; Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core.

D,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.

D-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily.

D,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.

ADP-heptose:LPS heptosyl transferase I; Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA; Belongs to the glycosyltransferase 9 family.

D,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.

UDP-glucose:(heptosyl)lipopolysaccharide alpha-1,3-glucosyltransferase; Involved in the addition of the first glucose residue to the lipopolysaccharide core; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

D,D-heptose 1,7-bisphosphate phosphatase; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.

Kinase that phosphorylates core heptose of lipopolysaccharide; Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core.

Myristoyl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2- (lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.

Bifunctional aspartokinase/homoserine dehydrogenase 2; Aspartokinase II and homoserine dehydrogenase II; Protein involved in methionine biosynthetic process and homoserine biosynthetic process.

Myristoyl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2- (lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.

Periplasmic folding chaperone, has an inactive PPIase domain; PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr.