UniProt functional annotation for P52477



	UniProt functional annotation for P52477

UniProt code: P52477.

Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Function: The periplasmic linker 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. Required for assembly of the MexA/MexB/OprM complex. Implicated in the secretion of the siderophore pyoverdine.

Function: The ability to export antibiotics and solvents is dramatically decreased in the presence of the proton conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner membrane is required for efflux. It is thought that the MexB subunit is a proton antiporter.

Subunit: Component of the MexAB-OprM multidrug efflux complex composed of an unknown number of MexA subunits, MexB and an OprM homotrimer. The MexA subunits are thought to form a barrel between the MexB inner membrane transporter and the trimeric OprM outer membrane channel protein. The N-terminus of the MexA subunits are anchored to the inner membrane while the alpha-helices of each subunit are hypothesized to form the barrel which would allow substrates to pass directly from the cytoplasm/inner membrane to the external mileu. How the MexA subunits interact with OprM and MexB, and how the OprM channel is opened is unknown.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10671490}; Lipid-anchor {ECO:0000255|PROSITE- ProRule:PRU00303, ECO:0000269|PubMed:10671490}. Note=The membrane anchor is not necessary for antibiotic efflux as the protein is functional when targeted to the periplasm by a foreign signal peptide.

Induction: By growth under severe iron limitation.

Miscellaneous: In both X-ray crystal structures approximately the last 100 residues are not ordered.

Similarity: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.



Function:		The periplasmic linker 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. Required for assembly of the MexA/MexB/OprM complex. Implicated in the secretion of the siderophore pyoverdine.



Function:		The ability to export antibiotics and solvents is dramatically decreased in the presence of the proton conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner membrane is required for efflux. It is thought that the MexB subunit is a proton antiporter.


Subunit:		Component of the MexAB-OprM multidrug efflux complex composed of an unknown number of MexA subunits, MexB and an OprM homotrimer. The MexA subunits are thought to form a barrel between the MexB inner membrane transporter and the trimeric OprM outer membrane channel protein. The N-terminus of the MexA subunits are anchored to the inner membrane while the alpha-helices of each subunit are hypothesized to form the barrel which would allow substrates to pass directly from the cytoplasm/inner membrane to the external mileu. How the MexA subunits interact with OprM and MexB, and how the OprM channel is opened is unknown.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:10671490}; Lipid-anchor {ECO:0000255\|PROSITE- ProRule:PRU00303, ECO:0000269\|PubMed:10671490}. Note=The membrane anchor is not necessary for antibiotic efflux as the protein is functional when targeted to the periplasm by a foreign signal peptide.
Induction:		By growth under severe iron limitation.
Miscellaneous:		In both X-ray crystal structures approximately the last 100 residues are not ordered.
Similarity:		Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. {ECO:0000305}.