Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family.

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family.

Mechanosensitive channel protein, high conductance; Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell disruption and death. The force required to trigger channel opening depends on the membrane lipids composition.

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family.

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Glycerol facilitator; Transporter of glycerol across the cytoplasmic membrane, with limited permeability to water and small uncharged compounds such as polyols; Belongs to the MIP/aquaporin (TC 1.A.8) family.

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Mechanosensitive channel protein, high conductance; Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell disruption and death. The force required to trigger channel opening depends on the membrane lipids composition.

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Mechanosensitive channel protein, small conductance; Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activ [...]

Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.

Outer membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...]

Arginine transporter subunit; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.

Arginine ABC transporter periplasmic binding protein; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.

Arginine transporter subunit; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.

Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family.

Arginine transporter subunit; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.

Glutamine transporter subunit; Involved in a glutamine-transport system GlnHPQ.

Arginine transporter subunit; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.

Outer membrane porin G; Forms channels functionally larger than those of classical porins.

Arginine ABC transporter periplasmic binding protein; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.

Arginine transporter subunit; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport.

Arginine ABC transporter periplasmic binding protein; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.

Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family.

Arginine ABC transporter periplasmic binding protein; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.

Glutamine transporter subunit; Involved in a glutamine-transport system GlnHPQ.

Arginine ABC transporter periplasmic binding protein; Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.

Outer membrane porin G; Forms channels functionally larger than those of classical porins.

F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

F0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.

F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

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.

F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.

F1 sector of membrane-bound ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

F0 sector of membrane-bound ATP synthase, subunit c; 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, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

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.