Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

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

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Regulatory protein sensor for oxidative stress; Regulates intracellular hydrogen peroxide (LysR family); similar to E. coli activator, hydrogen peroxide-inducible genes (AAC76943.1); Blastp hit to AAC76943.1 (305 aa), 95% identity in aa 1 - 305; Belongs to the LysR transcriptional regulatory family.

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...]

Putative heavy metal transcriptional repressor (MerR family); Regulates the transcription of the copA and cuiD (cueO) genes. Detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.

RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).

Similar to E. coli 5-aminolevulinate dehydratase = porphobilinogen synthase (AAC73472.1); Blastp hit to AAC73472.1 (335 aa), 93% identity in aa 12 - 335; Belongs to the ALAD family.

Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.

Similar to E. coli 5-aminolevulinate dehydratase = porphobilinogen synthase (AAC73472.1); Blastp hit to AAC73472.1 (335 aa), 93% identity in aa 12 - 335; Belongs to the ALAD family.

O2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.

Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.

Similar to E. coli 5-aminolevulinate dehydratase = porphobilinogen synthase (AAC73472.1); Blastp hit to AAC73472.1 (335 aa), 93% identity in aa 12 - 335; Belongs to the ALAD family.

Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.

O2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.

O2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.

Similar to E. coli 5-aminolevulinate dehydratase = porphobilinogen synthase (AAC73472.1); Blastp hit to AAC73472.1 (335 aa), 93% identity in aa 12 - 335; Belongs to the ALAD family.

O2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.

Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

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

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Regulatory protein sensor for oxidative stress; Regulates intracellular hydrogen peroxide (LysR family); similar to E. coli activator, hydrogen peroxide-inducible genes (AAC76943.1); Blastp hit to AAC76943.1 (305 aa), 95% identity in aa 1 - 305; Belongs to the LysR transcriptional regulatory family.

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity).

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

Bacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

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

Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

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

Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.