Also known as Outer membrane protein (OMPC).
Growth enhancer.

Also known as Outer membrane protein 40 (Omp40) (PG33).
May have porin activity and function in peptidoglycan binding.

Also known as Outer membrane protein 41 (Omp41) (PG32).
May have porin activity and function in peptidoglycan binding.

Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes ().

Could be involved in the transport of substrates.

Links the outer membrane to the inner membrane. Long fibrous protein that could serve to separate the two membranes.

Also known as Outer membrane protein C (Outer membrane protein 1B) (Porin OmpC).
Forms pores that allow passive diffusion of small molecules across the outer membrane.

Also known as Outer membrane protein F (Outer membrane protein 1A) (Outer membrane protein B) (Outer membrane protein IA) (Porin OmpF).
Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2 ().

Forms channels functionally larger than those of classical porins.

Also known as Outer membrane protein IIIA (OMPIIIA).
May act as an outer membrane pore.

Also known as Outer membrane protein lom (ORF 206A).
Incorporated into the outer membrane of the host during infection. Lom is expressed during lysogeny in E.coli.

Also known as Outer membrane protein MIP (Macrophage infectivity potentiator) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase).
Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.

Enzyme and pathway databasesBioCyc Collection of Pathway/Genome Databases<br/><a href='/database/5'>More..</a>BioCyciMTBCDC1551:GT3Z-6429-MONOMER.

Necessary for the secretion of IPA invasins.

Also known as Outer membrane protein N (Porin OmpN).
Forms pores that allow passive diffusion of small molecules across the outer membrane (). Non-specific porin.

Porin. Induces apoptosis in human cells through caspases-dependent and AIF-dependent pathways. Purified Omp38 enters the cells and localizes to the mitochondria, which leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor) ().

May play an important role in maintaining pathogenicity in plants.

Serves as receptor for a broad-host-range vibriophage, KVP40.

Enzyme and pathway databasesBioCyc Collection of Pathway/Genome Databases<br/><a href='/database/5'>More..</a>BioCyciVCHO:VC1318-MONOMER.

Channel-forming component of a multidrug resistance efflux pump.

The outer membrane component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Can replace the OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics exported are those exported by the intact MexCD pump, showing that efflux substrate specificity is not conferred by this component. Serves as the outer membrane component for the MexXY efflux system. Implicated in the secretion of the siderophore pyoverdine. OprM is probably involved in the efflux of the siderophore across the outer membrane.

Also known as Outer membrane protein P.IIC (Protein IIC).
This protein serves as a porin.

Able to form a pore in lipid bilayers.

Also known as Outer membrane protein P5 (OMP P5).

Also known as Outer membrane protein P6 (OMP P6) (15 kDa peptidoglycan-associated lipoprotein) (PC protein).
Thought to play a role in bacterial envelope integrity. Links the outer membrane to the peptidoglycan layer.

Also known as Outer membrane protein PagN (Adhesin/invasin protein PagN).
Haemagglutinin that facilitates the adhesion to and invasion of epithelial mammalian cells. Utilizes heparinated proteoglycan as a receptor to successfully invade host cells.

Enzyme and pathway databasesBioCyc Collection of Pathway/Genome Databases<br/><a href='/database/5'>More..</a>BioCyciMTBH37RV:G185E-6172-MONOMER.

Forms pores that allow passive diffusion of small molecules across the outer membrane.

Forms pores that allow passive diffusion of small molecules across the outer membrane.

The induction of slp may help to stabilize the outer membrane during carbon starvation and stationary phase.

Also known as Outer membrane protein SusE (Starch-utilization system protein E).
Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.

Also known as Outer membrane protein SusF (Starch-utilization system protein F).
Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has lower affinity for starch compared to SusE.

Also known as Outer membrane protein TolC (Multidrug efflux pump subunit TolC).
Outer membrane channel, which is required for the function of several efflux systems (). Required for virulence.

Also known as Outer membrane protein TP0453 (30kLP).
Might be involved in ligand transport, alters membrane permeability at acidic pH (4.0 to 5.5) (PubMed:21965687). Incubation of the non-lipidated form with lipid vesicles increases their permeability (PubMed:16159783).

Also known as Outer membrane protein Tpn50 (Antigen Tpp57).
Could function as a porin.

Also known as Outer membrane protein U (Porin OmpU).
Forms pores that allow passive diffusion of small molecules across the outer membrane.

Acts as a receptor for colicin S4.

Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues.

Also known as Outer membrane protein YopN (LcrE) (Yop4b).
Plays a major role in regulation of the low-calcium response. Seems to sense the calcium concentration and to transmit a signal to shut off yop transcription when the calcium concentration is high.