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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)DescriptionActionsGraphical viewLength
Topological domaini1 – 9Cytoplasmic1 Publication9
Transmembranei10 – 28HelicalAdd BLAST19
Topological domaini29 – 339Periplasmic1 PublicationAdd BLAST311
Transmembranei340 – 359HelicalAdd BLAST20
Topological domaini360 – 365Cytoplasmic1 Publication6
Transmembranei366 – 385HelicalAdd BLAST20
Topological domaini386 – 391Periplasmic1 Publication6
Transmembranei392 – 413HelicalAdd BLAST22
Topological domaini414 – 441Cytoplasmic1 PublicationAdd BLAST28
Transmembranei442 – 460HelicalAdd BLAST19
Topological domaini461 – 473Periplasmic1 PublicationAdd BLAST13
Transmembranei474 – 496HelicalAdd BLAST23
Topological domaini497 – 538Cytoplasmic1 PublicationAdd BLAST42
Transmembranei539 – 557HelicalAdd BLAST19
Topological domaini558 – 871Periplasmic1 PublicationAdd BLAST314
Transmembranei872 – 891HelicalAdd BLAST20
Topological domaini892 – 897Cytoplasmic1 Publication6
Transmembranei898 – 917HelicalAdd BLAST20
Topological domaini918 – 923Periplasmic1 Publication6
Transmembranei924 – 945HelicalAdd BLAST22
Topological domaini946 – 972Cytoplasmic1 PublicationAdd BLAST27
Transmembranei973 – 991HelicalAdd BLAST19
Topological domaini992 – 1004Periplasmic1 PublicationAdd BLAST13
Transmembranei1005 – 1027HelicalAdd BLAST23
Topological domaini1028 – 1046Cytoplasmic1 PublicationAdd BLAST19

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001618441 – 1046Multidrug resistance protein MexBAdd BLAST1046

Proteomic databases

PaxDbiP52002.
PRIDEiP52002.

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 interactors.
STRINGi208964.PA0426.

Structurei

Secondary structure

11046
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 7Combined sources6
Helixi9 – 27Combined sources19
Beta strandi42 – 48Combined sources7
Helixi54 – 60Combined sources7
Helixi62 – 66Combined sources5
Beta strandi75 – 83Combined sources9
Beta strandi86 – 94Combined sources9
Helixi100 – 114Combined sources15
Helixi115 – 117Combined sources3
Helixi120 – 123Combined sources4
Beta strandi128 – 143Combined sources16
Beta strandi145 – 147Combined sources3
Helixi151 – 161Combined sources11
Helixi163 – 167Combined sources5
Beta strandi172 – 179Combined sources8
Beta strandi182 – 188Combined sources7
Helixi190 – 195Combined sources6
Helixi200 – 210Combined sources11
Beta strandi233 – 235Combined sources3
Helixi243 – 247Combined sources5
Beta strandi250 – 252Combined sources3
Turni255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Helixi262 – 265Combined sources4
Beta strandi266 – 273Combined sources8
Beta strandi278 – 281Combined sources4
Beta strandi284 – 294Combined sources11
Helixi299 – 311Combined sources13
Helixi314 – 316Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi326 – 329Combined sources4
Helixi330 – 359Combined sources30
Helixi362 – 386Combined sources25
Helixi392 – 405Combined sources14
Helixi407 – 421Combined sources15
Helixi427 – 436Combined sources10
Helixi439 – 450Combined sources12
Turni451 – 453Combined sources3
Helixi455 – 457Combined sources3
Helixi461 – 496Combined sources36
Helixi513 – 537Combined sources25
Helixi539 – 555Combined sources17
Beta strandi571 – 577Combined sources7
Helixi584 – 600Combined sources17
Turni601 – 605Combined sources5
Beta strandi606 – 614Combined sources9
Turni621 – 623Combined sources3
Beta strandi624 – 631Combined sources8
Helixi634 – 636Combined sources3
Turni639 – 641Combined sources3
Beta strandi642 – 644Combined sources3
Helixi645 – 648Combined sources4
Turni649 – 651Combined sources3
Helixi652 – 656Combined sources5
Beta strandi659 – 666Combined sources8
Helixi672 – 674Combined sources3
Beta strandi676 – 679Combined sources4
Beta strandi682 – 685Combined sources4
Beta strandi688 – 690Combined sources3
Helixi692 – 705Combined sources14
Beta strandi716 – 719Combined sources4
Beta strandi726 – 730Combined sources5
Helixi732 – 738Combined sources7
Helixi742 – 753Combined sources12
Beta strandi756 – 763Combined sources8
Beta strandi766 – 774Combined sources9
Helixi776 – 778Combined sources3
Beta strandi779 – 781Combined sources3
Helixi782 – 786Combined sources5
Beta strandi789 – 791Combined sources3
Beta strandi793 – 795Combined sources3
Beta strandi797 – 799Combined sources3
Helixi800 – 802Combined sources3
Beta strandi803 – 807Combined sources5
Beta strandi813 – 815Combined sources3
Beta strandi816 – 827Combined sources12
Turni836 – 838Combined sources3
Helixi839 – 846Combined sources8
Helixi847 – 849Combined sources3
Beta strandi856 – 858Combined sources3
Helixi860 – 867Combined sources8
Helixi875 – 890Combined sources16
Beta strandi893 – 895Combined sources3
Helixi898 – 901Combined sources4
Turni902 – 904Combined sources3
Helixi905 – 916Combined sources12
Turni917 – 919Combined sources3
Helixi924 – 939Combined sources16
Helixi942 – 951Combined sources10
Helixi958 – 988Combined sources31
Helixi995 – 1023Combined sources29
Helixi1025 – 1028Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti29S → N in AAD45628 (PubMed:9989496).Curated1
Sequence conflicti90I → T in AAA74437 (PubMed:7968531).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

Proteomic databases

PaxDbiP52002.
PRIDEiP52002.

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: November 2, 2016
This is version 111 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.