Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Copper/silver efflux system, outer membrane component; Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.

Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Cytochrome o ubiquinol oxidase subunit II; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.

Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Anaerobic multidrug efflux transporter, ArcA-regulated; Part of the tripartite efflux system MdtEF-TolC, which confers resistance to compounds such as rhodamine 6G, erythromycin, doxorubicin, ethidium bromide, TPP, SDS, deoxycholate, crystal violet and benzalkonium; Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Outer membrane factor of efflux pump; Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Copper/silver efflux system, outer membrane component; Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Outer membrane factor of efflux pump; Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Cytoplasmic membrane lipoprotein-28; Lipoprotein-28.

Cytoplasmic membrane lipoprotein; Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.

Activator of AmiC murein hydrolase activity, lipoprotein; Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division.

1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; OM lipoprotein.

Activator of AmiC murein hydrolase activity, lipoprotein; Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division.

1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; OM lipoprotein.

Septal ring protein, suppressor of prc, minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family.

1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; OM lipoprotein.

Putative lipoprotein.

Putative thiamine-synthetic flavin transferase lipoprotein; Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex.

OM lipoprotein stimulator of MrcB transpeptidase; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b.

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete a [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

Lipoprotein component of BamABCDE OM biogenesis complex; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substr [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

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.

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

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 [...]

BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]

LPS assembly OM complex LptDE, lipoprotein component; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. Belongs to the LptE lipoprotein family.