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Protein

Multidrug resistance protein MexB

Gene

mexB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.
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.

GO - Molecular functioni

  • drug transmembrane transporter activity Source: PseudoCAP

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Protein family/group databases

TCDBi2.A.6.2.6. the resistance-nodulation-cell division (rnd) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug resistance protein MexB
Alternative name(s):
Multidrug-efflux transporter MexB
Gene namesi
Name:mexB
Ordered Locus Names:PA0426
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0426.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic1 Publication
Transmembranei10 – 2819HelicalAdd
BLAST
Topological domaini29 – 339311Periplasmic1 PublicationAdd
BLAST
Transmembranei340 – 35920HelicalAdd
BLAST
Topological domaini360 – 3656Cytoplasmic1 Publication
Transmembranei366 – 38520HelicalAdd
BLAST
Topological domaini386 – 3916Periplasmic1 Publication
Transmembranei392 – 41322HelicalAdd
BLAST
Topological domaini414 – 44128Cytoplasmic1 PublicationAdd
BLAST
Transmembranei442 – 46019HelicalAdd
BLAST
Topological domaini461 – 47313Periplasmic1 PublicationAdd
BLAST
Transmembranei474 – 49623HelicalAdd
BLAST
Topological domaini497 – 53842Cytoplasmic1 PublicationAdd
BLAST
Transmembranei539 – 55719HelicalAdd
BLAST
Topological domaini558 – 871314Periplasmic1 PublicationAdd
BLAST
Transmembranei872 – 89120HelicalAdd
BLAST
Topological domaini892 – 8976Cytoplasmic1 Publication
Transmembranei898 – 91720HelicalAdd
BLAST
Topological domaini918 – 9236Periplasmic1 Publication
Transmembranei924 – 94522HelicalAdd
BLAST
Topological domaini946 – 97227Cytoplasmic1 PublicationAdd
BLAST
Transmembranei973 – 99119HelicalAdd
BLAST
Topological domaini992 – 100413Periplasmic1 PublicationAdd
BLAST
Transmembranei1005 – 102723HelicalAdd
BLAST
Topological domaini1028 – 104619Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10461046Multidrug resistance protein MexBPRO_0000161844Add
BLAST

Proteomic databases

PaxDbiP52002.

Expressioni

Inductioni

By growth under severe iron limitation.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
arcAP0A9Q12EBI-6400435,EBI-1119939From a different organism.

Protein-protein interaction databases

DIPiDIP-60510N.
IntActiP52002. 2 interactions.
STRINGi208964.PA0426.

Structurei

Secondary structure

1
1046
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 76Combined sources
Helixi9 – 2719Combined sources
Beta strandi42 – 487Combined sources
Helixi54 – 607Combined sources
Helixi62 – 665Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 949Combined sources
Helixi100 – 11415Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 1234Combined sources
Beta strandi128 – 14316Combined sources
Beta strandi145 – 1473Combined sources
Helixi151 – 16111Combined sources
Helixi163 – 1675Combined sources
Beta strandi172 – 1798Combined sources
Beta strandi182 – 1887Combined sources
Helixi190 – 1956Combined sources
Helixi200 – 21011Combined sources
Beta strandi233 – 2353Combined sources
Helixi243 – 2475Combined sources
Beta strandi250 – 2523Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2613Combined sources
Helixi262 – 2654Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi278 – 2814Combined sources
Beta strandi284 – 29411Combined sources
Helixi299 – 31113Combined sources
Helixi314 – 3163Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi326 – 3294Combined sources
Helixi330 – 35930Combined sources
Helixi362 – 38625Combined sources
Helixi392 – 40514Combined sources
Helixi407 – 42115Combined sources
Helixi427 – 43610Combined sources
Helixi439 – 45012Combined sources
Turni451 – 4533Combined sources
Helixi455 – 4573Combined sources
Helixi461 – 49636Combined sources
Helixi513 – 53725Combined sources
Helixi539 – 55517Combined sources
Beta strandi571 – 5777Combined sources
Helixi584 – 60017Combined sources
Turni601 – 6055Combined sources
Beta strandi606 – 6149Combined sources
Turni621 – 6233Combined sources
Beta strandi624 – 6318Combined sources
Helixi634 – 6363Combined sources
Turni639 – 6413Combined sources
Beta strandi642 – 6443Combined sources
Helixi645 – 6484Combined sources
Turni649 – 6513Combined sources
Helixi652 – 6565Combined sources
Beta strandi659 – 6668Combined sources
Helixi672 – 6743Combined sources
Beta strandi676 – 6794Combined sources
Beta strandi682 – 6854Combined sources
Beta strandi688 – 6903Combined sources
Helixi692 – 70514Combined sources
Beta strandi716 – 7194Combined sources
Beta strandi726 – 7305Combined sources
Helixi732 – 7387Combined sources
Helixi742 – 75312Combined sources
Beta strandi756 – 7638Combined sources
Beta strandi766 – 7749Combined sources
Helixi776 – 7783Combined sources
Beta strandi779 – 7813Combined sources
Helixi782 – 7865Combined sources
Beta strandi789 – 7913Combined sources
Beta strandi793 – 7953Combined sources
Beta strandi797 – 7993Combined sources
Helixi800 – 8023Combined sources
Beta strandi803 – 8075Combined sources
Beta strandi813 – 8153Combined sources
Beta strandi816 – 82712Combined sources
Turni836 – 8383Combined sources
Helixi839 – 8468Combined sources
Helixi847 – 8493Combined sources
Beta strandi856 – 8583Combined sources
Helixi860 – 8678Combined sources
Helixi875 – 89016Combined sources
Beta strandi893 – 8953Combined sources
Helixi898 – 9014Combined sources
Turni902 – 9043Combined sources
Helixi905 – 91612Combined sources
Turni917 – 9193Combined sources
Helixi924 – 93916Combined sources
Helixi942 – 95110Combined sources
Helixi958 – 98831Combined sources
Helixi995 – 102329Combined sources
Helixi1025 – 10284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V50X-ray3.00A/B/C/D/E/F1-1046[»]
3W9IX-ray2.71A/B/C/D/E/F1-1046[»]
3W9JX-ray3.15A/B/C/D/E/F1-1046[»]
ProteinModelPortaliP52002.
SMRiP52002. Positions 1-1033.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52002.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZS. Bacteria.
COG0841. LUCA.
InParanoidiP52002.
KOiK18138.
OMAiYASGQME.
PhylomeDBiP52002.

Family and domain databases

Gene3Di3.30.2090.10. 2 hits.
InterProiIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
PfamiPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSiPR00702. ACRIFLAVINRP.
SUPFAMiSSF82714. SSF82714. 2 hits.
TIGRFAMsiTIGR00915. 2A0602. 1 hit.

Sequencei

Sequence statusi: Complete.

P52002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKFFIDRPI FAWVIALVIM LAGGLSILSL PVNQYPAIAP PAIAVQVSYP
60 70 80 90 100
GASAETVQDT VVQVIEQQMN GIDNLRYISS ESNSDGSMTI TVTFEQGTDP
110 120 130 140 150
DIAQVQVQNK LQLATPLLPQ EVQRQGIRVT KAVKNFLMVV GVVSTDGSMT
160 170 180 190 200
KEDLSNYIVS NIQDPLSRTK GVGDFQVFGS QYSMRIWLDP AKLNSYQLTP
210 220 230 240 250
GDVSSAIQAQ NVQISSGQLG GLPAVKGQQL NATIIGKTRL QTAEQFENIL
260 270 280 290 300
LKVNPDGSQV RLKDVADVGL GGQDYSINAQ FNGSPASGIA IKLATGANAL
310 320 330 340 350
DTAKAIRQTI ANLEPFMPQG MKVVYPYDTT PVVSASIHEV VKTLGEAILL
360 370 380 390 400
VFLVMYLFLQ NFRATLIPTI AVPVVLLGTF GVLAAFGFSI NTLTMFGMVL
410 420 430 440 450
AIGLLVDDAI VVVENVERVM AEEGLSPREA ARKSMGQIQG ALVGIAMVLS
460 470 480 490 500
AVFLPMAFFG GSTGVIYRQF SITIVSAMAL SVIVALILTP ALCATMLKPI
510 520 530 540 550
EKGDHGEHKG GFFGWFNRMF LSTTHGYERG VASILKHRAP YLLIYVVIVA
560 570 580 590 600
GMIWMFTRIP TAFLPDEDQG VLFAQVQTPP GSSAERTQVV VDSMREYLLE
610 620 630 640 650
KESSSVSSVF TVTGFNFAGR GQSSGMAFIM LKPWEERPGG ENSVFELAKR
660 670 680 690 700
AQMHFFSFKD AMVFAFAPPS VLELGNATGF DLFLQDQAGV GHEVLLQARN
710 720 730 740 750
KFLMLAAQNP ALQRVRPNGM SDEPQYKLEI DDEKASALGV SLADINSTVS
760 770 780 790 800
IAWGSSYVND FIDRGRVKRV YLQGRPDARM NPDDLSKWYV RNDKGEMVPF
810 820 830 840 850
NAFATGKWEY GSPKLERYNG VPAMEILGEP APGLSSGDAM AAVEEIVKQL
860 870 880 890 900
PKGVGYSWTG LSYEERLSGS QAPALYALSL LVVFLCLAAL YESWSIPFSV
910 920 930 940 950
MLVVPLGVIG ALLATSMRGL SNDVFFQVGL LTTIGLSAKN AILIVEFAKE
960 970 980 990 1000
LHEQGKGIVE AAIEACRMRL RPIVMTSLAF ILGVVPLAIS TGAGSGSQHA
1010 1020 1030 1040
IGTGVIGGMV TATVLAIFWV PLFYVAVSTL FKDEASKQQA SVEKGQ
Length:1,046
Mass (Da):112,791
Last modified:December 8, 2000 - v2
Checksum:iFF91855338868ED2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291S → N in AAD45628 (PubMed:9989496).Curated
Sequence conflicti90 – 901I → T in AAA74437 (PubMed:7968531).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11616 Genomic DNA. Translation: AAA74437.1.
AE004091 Genomic DNA. Translation: AAG03815.1.
AF092566 Genomic DNA. Translation: AAD45628.1.
PIRiE83593.
S39630.
RefSeqiNP_249117.1. NC_002516.2.
WP_003107312.1. NZ_ASJY01000084.1.

Genome annotation databases

EnsemblBacteriaiAAG03815; AAG03815; PA0426.
GeneIDi877852.
KEGGipae:PA0426.
PATRICi19835094. VBIPseAer58763_0448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11616 Genomic DNA. Translation: AAA74437.1.
AE004091 Genomic DNA. Translation: AAG03815.1.
AF092566 Genomic DNA. Translation: AAD45628.1.
PIRiE83593.
S39630.
RefSeqiNP_249117.1. NC_002516.2.
WP_003107312.1. NZ_ASJY01000084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V50X-ray3.00A/B/C/D/E/F1-1046[»]
3W9IX-ray2.71A/B/C/D/E/F1-1046[»]
3W9JX-ray3.15A/B/C/D/E/F1-1046[»]
ProteinModelPortaliP52002.
SMRiP52002. Positions 1-1033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60510N.
IntActiP52002. 2 interactions.
STRINGi208964.PA0426.

Protein family/group databases

TCDBi2.A.6.2.6. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbiP52002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG03815; AAG03815; PA0426.
GeneIDi877852.
KEGGipae:PA0426.
PATRICi19835094. VBIPseAer58763_0448.

Organism-specific databases

PseudoCAPiPA0426.

Phylogenomic databases

eggNOGiENOG4105BZS. Bacteria.
COG0841. LUCA.
InParanoidiP52002.
KOiK18138.
OMAiYASGQME.
PhylomeDBiP52002.

Miscellaneous databases

EvolutionaryTraceiP52002.

Family and domain databases

Gene3Di3.30.2090.10. 2 hits.
InterProiIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
PfamiPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSiPR00702. ACRIFLAVINRP.
SUPFAMiSSF82714. SSF82714. 2 hits.
TIGRFAMsiTIGR00915. 2A0602. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMEXB_PSEAE
AccessioniPrimary (citable) accession number: P52002
Secondary accession number(s): Q9S505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 8, 2000
Last modified: September 7, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.