CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.

Heme export ABC transporter ATPase; Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.

CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.

Ferrienterobactin ABC transporter periplasmic binding protein; Binds ferrienterobactin; part of the binding-protein- dependent transport system for uptake of ferrienterobactin.

CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.

Ferrienterobactin ABC transporter ATPase; Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for energy coupling to the transport system.

CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.

Iron(3+)-hydroxamate import ABC transporter permease; Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane.

CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.

Iron(3+)-hydroxamate import ABC transporter periplasmic binding protein; Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Colicin IA outer membrane receptor and translocator; Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Fe-binding and storage protein; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and cop [...]

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Ferrous iron transporter, protein A; Involved in Fe(2+) ion uptake. Does not stimulate the GTPase activity of the N-terminus of FeoB (residues 1- 276).

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Ferrous iron transporter protein B and GTP-binding protein; Transporter of a GTP-driven Fe(2+) uptake system, probably couples GTP-binding to channel opening and Fe(2+) uptake. A guanine nucleotide-binding protein (G proteins) in which the guanine nucleotide binding site alternates between an active, GTP-bound state and an inactive, GDP- bound state. This protein has fast intrinsic GDP release, mediated by the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads to conformational changes and channel closing. A GDP release mechanism involving a conformational change of the [...]

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Ferritin iron storage protein (cytoplasmic); Iron-storage protein; Belongs to the ferritin family. Prokaryotic subfamily.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Ferritin B, putative ferrous iron reservoir; Ferritin-like protein; Protein involved in iron ion transport.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Iron-sulfur cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D- state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters; Belongs to the NifU family.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Fe/S biogenesis protein, putative scaffold/chaperone protein; Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Belongs to the NfuA family.

Bacterioferritin, iron storage and detoxification protein; 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. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.

Membrane spanning protein in TonB-ExbB-ExbD transport complex; 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 tran [...]

Stationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...]

Fe-binding and storage protein; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and cop [...]

Stationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...]

Glutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily.

Stationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...]

Acid stress protein; Involved in cell resistance against acid stress.

Stationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...]

Iron-sulfur cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D- state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters; Belongs to the NifU family.

Stationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...]

Fe/S biogenesis protein, putative scaffold/chaperone protein; Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Belongs to the NfuA family.

Heme export ABC transporter ATPase; Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.

CP4-6 prophage; Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system.