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.

FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

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.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

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.

30S ribosomal subunit protein S2; Required for ribosomal protein S1 to bind to the 30S subunit.

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.

FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...]

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.

Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.

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.

Peptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily.

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.

Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

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.

FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...]

FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.

FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Peptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

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.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

Protein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA. HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa. May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Belongs to the HypA/HybF family.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

GTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...]

Protein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA. HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa. May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Belongs to the HypA/HybF family.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

Protein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA. HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa. May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Belongs to the HypA/HybF family.

GTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.

Protein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA. HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa. May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Belongs to the HypA/HybF family.

FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...]

GTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.

Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family.

GTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.

Protein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA. HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa. May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Belongs to the HypA/HybF family.