Putative ABC transporter permease; Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Putative ABC transporter permease; Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Putative ABC transporter permease; Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

Macrolide transporter membrane fusion protein (MFP) component; Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP- bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system co [...]

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Macrolide transporter membrane fusion protein (MFP) component; Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP- bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system co [...]

Transport channel; Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Putative ABC transporter permease; Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Macrolide transporter membrane fusion protein (MFP) component; Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP- bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system co [...]

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

Transport channel; Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.

ABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaB plays critical roles in both the assembly and activity of the complex. May act by modulating MlaF structure and stability.

OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.

ABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaB plays critical roles in both the assembly and activity of the complex. May act by modulating MlaF structure and stability.

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]

OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.

ABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaB plays critical roles in both the assembly and activity of the complex. May act by modulating MlaF structure and stability.

OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family.

Macrolide ABC transporter peremase/ATPase; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid. Belongs to the ABC transporter superfamily. Macrolide exporte [...]