Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein-releasing system transmembrane protein; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

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.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein-releasing system transmembrane protein; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Murein lipoprotein; An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most adundant cellular protein, there can be up to 10(6) Lpp molecules pe [...]

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Prolipoprotein signal peptidase (signal peptidase II); This protein specifically catalyzes the removal of signal peptides from prolipoproteins.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

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 [...]

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Lipoprotein-releasing system transmembrane protein; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

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.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Lipoprotein-releasing system transmembrane protein; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Murein lipoprotein; An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most adundant cellular protein, there can be up to 10(6) Lpp molecules pe [...]

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Prolipoprotein signal peptidase (signal peptidase II); This protein specifically catalyzes the removal of signal peptides from prolipoproteins.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

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 [...]

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family.

Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...]

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family.

Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family.

Lipoprotein-releasing system transmembrane protein; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.

Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB 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.