| General information | | DisProt: | DP00401 | | Name: | Multidrug resistance protein mexA | | Synonym(s): | MEXA_PSEAE
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P52477 | | UniGene: | | | SwissProt: | MEXA_PSEAE | | TrEMBL: | | | NCBI (GI): | 1709008 | | Source organism: | Pseudomonas aeruginosa | | Sequence length: | 383 | | Percent disordered: | 34% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MQRTPAMRVL VPALLVAISA LSGCGKSEAP PPAQTPEVGI VTLEAQTVTL NTELPGRTNA - 60
FRIAEVRPQV NGIILKRLFK EGSDVKAGQQ LYQIDPATYE ADYQSAQANL ASTQEQAQRY - 120
KLLVADQAVS KQQYADANAA YLQSKAAVEQ ARINLRYTKV LSPISGRIGR SAVTEGALVT - 180
NGQANAMATV QQLDPIYVDV TQPSTALLRL RRELASGQLE RAGDNAAKVS LKLEDGSQYP - 240
LEGRLEFSEV SVDEGTGSVT IRAVFPNPNN ELLPGMFVHA QLQEGVKQKA ILAPQQGVTR - 300
DLKGQATALV VNAQNKVELR VIKADRVIGD KWLVTEGLNA GDKIITEGLQ FVQPGVEVKT - 360
VPAKNVASAQ KADAAPAKTD SKG
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| Functional narrative |
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. 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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 24 - 51 | | Length: | 28 | | Region sequence: |
CGKSEAPPPAQTPEVGIVTLEAQTVTLN | | Modification type: | Fragment
Mutant
| | PDB: | 1T5E:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- X-ray crystallography (291 K; Ammonium sulfate 50 mM; n-tetradecyl-Beta-D-maltoside 0.1 mM; PEG 3350 (10%))
| References:
- Higgins MK, Bokma E, Koronakis E, Hughes C, Koronakis V. "Structure of the periplasmic component of a bacterial drug efflux pump." Proc Natl Acad Sci U S A. 2004; 101(27): 9994-9. PubMed: 15226509
| Comments:The mature protein, consisiting of resisdues 24-383, was used for structure determination. It also had a C24S mutation to prevent fatty acid attachment at the N-terminal.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 283 - 383 | | Length: | 101 | | Region sequence: |
QEGVKQKAILAPQQGVTRDLKGQATALVVNAQNKVELRVIKADRVIGDKWLVTEGLNAGD
KIITEGLQFVQPGVEVKTVPAKNVASAQKADAAPAKTDSKG | | Modification type: | Fragment
Mutant
| | PDB: | 1T5E:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- X-ray crystallography (291 K; Ammonium sulfate 50 mM; n-tetradecyl-Beta-D-maltoside 0.1 mM; PEG 3350 (10%))
| References:
- Higgins MK, Bokma E, Koronakis E, Hughes C, Koronakis V. "Structure of the periplasmic component of a bacterial drug efflux pump." Proc Natl Acad Sci U S A. 2004; 101(27): 9994-9. PubMed: 15226509
| Comments:The mature protein, consisiting of resisdues 24-383, was used for structure determination. It also had a C24S mutation to prevent fatty acid attachment at the N-terminal.
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