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P52002 (MEXB_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multidrug resistance protein MexB
Alternative name(s):
Multidrug-efflux transporter MexB
Gene names
Name:mexB
Ordered Locus Names:PA0426
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length1046 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The inner membrane transporter 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. Implicated in the secretion of the siderophore pyoverdine. Ref.5 Ref.6 Ref.7

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. Ref.5 Ref.6 Ref.7

Subunit structure

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 which allows substrates to pass directly from the cytoplasm 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; Multi-pass membrane protein.

Induction

By growth under severe iron limitation.

Sequence similarities

Belongs to the AcrB/AcrD/AcrF (TC 2.A.6) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10461046Multidrug resistance protein MexB
PRO_0000161844

Regions

Topological domain1 – 99Cytoplasmic Ref.8
Transmembrane10 – 2819Helical
Topological domain29 – 339311Periplasmic Ref.8
Transmembrane340 – 35920Helical
Topological domain360 – 3656Cytoplasmic Ref.8
Transmembrane366 – 38520Helical
Topological domain386 – 3916Periplasmic Ref.8
Transmembrane392 – 41322Helical
Topological domain414 – 44128Cytoplasmic Ref.8
Transmembrane442 – 46019Helical
Topological domain461 – 47313Periplasmic Ref.8
Transmembrane474 – 49623Helical
Topological domain497 – 53842Cytoplasmic Ref.8
Transmembrane539 – 55719Helical
Topological domain558 – 871314Periplasmic Ref.8
Transmembrane872 – 89120Helical
Topological domain892 – 8976Cytoplasmic Ref.8
Transmembrane898 – 91720Helical
Topological domain918 – 9236Periplasmic Ref.8
Transmembrane924 – 94522Helical
Topological domain946 – 97227Cytoplasmic Ref.8
Transmembrane973 – 99119Helical
Topological domain992 – 100413Periplasmic Ref.8
Transmembrane1005 – 102723Helical
Topological domain1028 – 104619Cytoplasmic Ref.8

Experimental info

Sequence conflict291S → N in AAD45628. Ref.3
Sequence conflict901I → T in AAA74437. Ref.1

Secondary structure

1 ................................................................................................................................................... 1046
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52002 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: FF91855338868ED2

FASTA1,046112,791
        10         20         30         40         50         60 
MSKFFIDRPI FAWVIALVIM LAGGLSILSL PVNQYPAIAP PAIAVQVSYP GASAETVQDT 

        70         80         90        100        110        120 
VVQVIEQQMN GIDNLRYISS ESNSDGSMTI TVTFEQGTDP DIAQVQVQNK LQLATPLLPQ 

       130        140        150        160        170        180 
EVQRQGIRVT KAVKNFLMVV GVVSTDGSMT KEDLSNYIVS NIQDPLSRTK GVGDFQVFGS 

       190        200        210        220        230        240 
QYSMRIWLDP AKLNSYQLTP GDVSSAIQAQ NVQISSGQLG GLPAVKGQQL NATIIGKTRL 

       250        260        270        280        290        300 
QTAEQFENIL LKVNPDGSQV RLKDVADVGL GGQDYSINAQ FNGSPASGIA IKLATGANAL 

       310        320        330        340        350        360 
DTAKAIRQTI ANLEPFMPQG MKVVYPYDTT PVVSASIHEV VKTLGEAILL VFLVMYLFLQ 

       370        380        390        400        410        420 
NFRATLIPTI AVPVVLLGTF GVLAAFGFSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM 

       430        440        450        460        470        480 
AEEGLSPREA ARKSMGQIQG ALVGIAMVLS AVFLPMAFFG GSTGVIYRQF SITIVSAMAL 

       490        500        510        520        530        540 
SVIVALILTP ALCATMLKPI EKGDHGEHKG GFFGWFNRMF LSTTHGYERG VASILKHRAP 

       550        560        570        580        590        600 
YLLIYVVIVA GMIWMFTRIP TAFLPDEDQG VLFAQVQTPP GSSAERTQVV VDSMREYLLE 

       610        620        630        640        650        660 
KESSSVSSVF TVTGFNFAGR GQSSGMAFIM LKPWEERPGG ENSVFELAKR AQMHFFSFKD 

       670        680        690        700        710        720 
AMVFAFAPPS VLELGNATGF DLFLQDQAGV GHEVLLQARN KFLMLAAQNP ALQRVRPNGM 

       730        740        750        760        770        780 
SDEPQYKLEI DDEKASALGV SLADINSTVS IAWGSSYVND FIDRGRVKRV YLQGRPDARM 

       790        800        810        820        830        840 
NPDDLSKWYV RNDKGEMVPF NAFATGKWEY GSPKLERYNG VPAMEILGEP APGLSSGDAM 

       850        860        870        880        890        900 
AAVEEIVKQL PKGVGYSWTG LSYEERLSGS QAPALYALSL LVVFLCLAAL YESWSIPFSV 

       910        920        930        940        950        960 
MLVVPLGVIG ALLATSMRGL SNDVFFQVGL LTTIGLSAKN AILIVEFAKE LHEQGKGIVE 

       970        980        990       1000       1010       1020 
AAIEACRMRL RPIVMTSLAF ILGVVPLAIS TGAGSGSQHA IGTGVIGGMV TATVLAIFWV 

      1030       1040 
PLFYVAVSTL FKDEASKQQA SVEKGQ

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine."
Poole K., Heinrichs D.E., Neshat S.
Mol. Microbiol. 10:529-544(1993) [PubMed: 7968531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAO6609.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model."
Mahajan-Miklos S., Tan M.-W., Rahme L.G., Ausubel F.M.
Cell 96:47-56(1999) [PubMed: 9989496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
Strain: PA14.
[4]"Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry."
Blonder J., Goshe M.B., Xiao W., Camp D.G. II, Wingerd M., Davis R.W., Smith R.D.
J. Proteome Res. 3:434-444(2004) [PubMed: 15253424] [Abstract]
Cited for: PROTEIN SEQUENCE OF 171-185; 240-252; 308-322 AND 818-848, MASS SPECTROMETRY.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[5]"Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon."
Poole K., Krebes K., McNally C., Neshat S.
J. Bacteriol. 175:7363-7372(1993) [PubMed: 8226684] [Abstract]
Cited for: FUNCTION AS AN ANTIBIOTIC EFFLUX PUMP.
Strain: PAO6609.
[6]"Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa."
Li X.-Z., Nikaido H., Poole K.
Antimicrob. Agents Chemother. 39:1948-1953(1995) [PubMed: 8540696] [Abstract]
Cited for: FUNCTION IN ANTIBIOTIC EFFLUX AND ENERGETIC REQUIREMENTS.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[7]"Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance."
Li X.-Z., Zhang L., Poole K.
J. Bacteriol. 180:2987-2991(1998) [PubMed: 9603892] [Abstract]
Cited for: FUNCTION IN SOLVENT EFFLUX.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[8]"Membrane topology of the xenobiotic-exporting subunit, MexB, of the MexA,B-OprM extrusion pump in Pseudomonas aeruginosa."
Guan L., Ehrmann M., Yoneyama H., Nakae T.
J. Biol. Chem. 274:10517-10522(1999) [PubMed: 10187844] [Abstract]
Cited for: TOPOLOGY.
Strain: PAO4290.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L11616 Genomic DNA. Translation: AAA74437.1.
AE004091 Genomic DNA. Translation: AAG03815.1.
AF092566 Genomic DNA. Translation: AAD45628.1.
PIRE83593.
S39630.
RefSeqNP_249117.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V50X-ray3.00A/B/C/D/E/F1-1046[»]
ProteinModelPortalP52002.
SMRP52002. Positions 4-1017.
ModBaseSearch...

Protein family/group databases

TCDB2.A.6.2.6. resistance-nodulation-cell division (RND) superfamily.

Proteomic databases

PRIDEP52002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID877852.
GenomeReviewsGene locus PA0426 in contig AE004091_GR.
KEGGpae:PA0426.
PATRIC19835094. VBIPseAer58763_0448.

Organism-specific databases

PseudoCAPPA0426.

Phylogenomic databases

HOGENOMHBG293864.
OMAWVPLFFV.
ProtClustDBCLSK865853.

Enzyme and pathway databases

BioCycPAER208964:PA0426-MONOMER.

Family and domain databases

InterProIPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
KOK03296.
PfamPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSPR00702. ACRIFLAVINRP.
TIGRFAMsTIGR00915. 2A0602. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMEXB_PSEAE
AccessionPrimary (citable) accession number: P52002
Secondary accession number(s): Q9S505
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 8, 2000
Last modified: January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents