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Protein

Multidrug efflux pump subunit AcrB

Gene

acrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates.4 Publications
Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its role in CDI is independent of the AcrA-AcrB-TolC efflux pump complex.1 Publication

GO - Molecular functioni

  • drug:proton antiporter activity Source: EcoCyc
  • drug transmembrane transporter activity Source: EcoCyc
  • efflux transmembrane transporter activity Source: InterPro
  • identical protein binding Source: IntAct

GO - Biological processi

Keywordsi

Biological processTransport

Enzyme and pathway databases

BioCyciEcoCyc:ACRB-MONOMER
MetaCyc:ACRB-MONOMER

Protein family/group databases

TCDBi2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug efflux pump subunit AcrB
Alternative name(s):
AcrAB-TolC multidrug efflux pump subunit AcrB
Acridine resistance protein B
Gene namesi
Name:acrB
Synonyms:acrE
Ordered Locus Names:b0462, JW0451
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11704 acrB

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 9Cytoplasmic1 Publication9
Transmembranei10 – 28Helical; Name=1Add BLAST19
Topological domaini29 – 336Periplasmic1 PublicationAdd BLAST308
Transmembranei337 – 356Helical; Name=2Add BLAST20
Topological domaini357 – 365Cytoplasmic1 Publication9
Transmembranei366 – 385Helical; Name=3Add BLAST20
Topological domaini386 – 391Periplasmic1 Publication6
Transmembranei392 – 413Helical; Name=4Add BLAST22
Topological domaini414 – 438Cytoplasmic1 PublicationAdd BLAST25
Transmembranei439 – 457Helical; Name=5Add BLAST19
Topological domaini458 – 465Periplasmic1 Publication8
Transmembranei466 – 490Helical; Name=6Add BLAST25
Topological domaini491 – 538Cytoplasmic1 PublicationAdd BLAST48
Transmembranei539 – 555Helical; Name=7Add BLAST17
Topological domaini556 – 871Periplasmic1 PublicationAdd BLAST316
Transmembranei872 – 888Helical; Name=8Add BLAST17
Topological domaini889 – 898Cytoplasmic1 Publication10
Transmembranei899 – 918Helical; Name=9Add BLAST20
Topological domaini919 – 924Periplasmic1 Publication6
Transmembranei925 – 943Helical; Name=10Add BLAST19
Topological domaini944 – 972Cytoplasmic1 PublicationAdd BLAST29
Transmembranei973 – 992Helical; Name=11Add BLAST20
Topological domaini993 – 998Periplasmic1 Publication6
Transmembranei999 – 1018Helical; Name=12Add BLAST20
Topological domaini1019 – 1049Cytoplasmic1 PublicationAdd BLAST31

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Loss of susceptibility to contact-dependent growth inhibition (CDI); inhibiting cells still contact the target.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi526H → Y: Partially restores chloramphenicol resistance to an AcrZ G30R mutant. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1681614
DrugBankiDB03619 Deoxycholic Acid
DB04209 Dequadin
DB03825 Rhodamine 6G

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001618111 – 1049Multidrug efflux pump subunit AcrBAdd BLAST1049

Proteomic databases

EPDiP31224
PaxDbiP31224
PRIDEiP31224

Expressioni

Inductioni

Positively regulated by MarA, Rob and SoxS transcriptional regulators (at protein level).1 Publication

Interactioni

Subunit structurei

Homotrimer, with large domains that extend into the periplasm, interacts with AcrA and TolC. AcrA may be required to stably link this protein and TolC. Interacts with AcrZ. Part of the AcrA-AcrB-AcrZ-TolC efflux pump.9 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4259859, 386 interactors
DIPiDIP-9049N
IntActiP31224, 9 interactors
MINTiP31224
STRINGi316385.ECDH10B_0418

Structurei

Secondary structure

11049
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP31224
SMRiP31224
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31224

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZS Bacteria
COG0841 LUCA
HOGENOMiHOG000158129
InParanoidiP31224
KOiK18138
PhylomeDBiP31224

Family and domain databases

Gene3Di3.30.2090.10, 2 hits
InterProiView protein in InterPro
IPR027463 AcrB_DN_DC_subdom
IPR001036 Acrflvin-R
IPR004764 HAE1
PANTHERiPTHR32063 PTHR32063, 1 hit
PfamiView protein in Pfam
PF00873 ACR_tran, 1 hit
PRINTSiPR00702 ACRIFLAVINRP
SUPFAMiSSF82714 SSF82714, 2 hits
TIGRFAMsiTIGR00915 2A0602, 1 hit

Sequencei

Sequence statusi: Complete.

P31224-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP
60 70 80 90 100
GADAKTVQDT VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA
110 120 130 140 150
DIAQVQVQNK LQLAMPLLPQ EVQQQGVSVE KSSSSFLMVV GVINTDGTMT
160 170 180 190 200
QEDISDYVAA NMKDAISRTS GVGDVQLFGS QYAMRIWMNP NELNKFQLTP
210 220 230 240 250
VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL TSTEEFGKIL
260 270 280 290 300
LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL
310 320 330 340 350
DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL
360 370 380 390 400
VFLVMYLFLQ NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL
410 420 430 440 450
AIGLLVDDAI VVVENVERVM AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS
460 470 480 490 500
AVFVPMAFFG GSTGAIYRQF SITIVSAMAL SVLVALILTP ALCATMLKPI
510 520 530 540 550
AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR YLVLYLIIVV
560 570 580 590 600
GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT
610 620 630 640 650
KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR
660 670 680 690 700
ATRAFSQIKD AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN
710 720 730 740 750
QLLAEAAKHP DMLTSVRPNG LEDTPQFKID IDQEKAQALG VSINDINTTL
760 770 780 790 800
GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR MLPDDIGDWY VRAADGQMVP
810 820 830 840 850
FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA MELMEQLASK
860 870 880 890 900
LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS
910 920 930 940 950
VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK
960 970 980 990 1000
DLMDKEGKGL IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ
1010 1020 1030 1040
NAVGTGVMGG MVTATVLAIF FVPVFFVVVR RRFSRKNEDI EHSHTVDHH
Length:1,049
Mass (Da):113,574
Last modified:July 1, 1993 - v1
Checksum:i19670E3C4CC29055
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94248 Genomic DNA Translation: AAA23411.1
U00734 Genomic DNA Translation: AAA67135.1
U82664 Genomic DNA Translation: AAB40216.1
U00096 Genomic DNA Translation: AAC73564.1
AP009048 Genomic DNA Translation: BAE76241.1
PIRiB36938
RefSeqiNP_414995.1, NC_000913.3
WP_001132469.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73564; AAC73564; b0462
BAE76241; BAE76241; BAE76241
GeneIDi945108
KEGGiecj:JW0451
eco:b0462
PATRICifig|1411691.4.peg.1814

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94248 Genomic DNA Translation: AAA23411.1
U00734 Genomic DNA Translation: AAA67135.1
U82664 Genomic DNA Translation: AAB40216.1
U00096 Genomic DNA Translation: AAC73564.1
AP009048 Genomic DNA Translation: BAE76241.1
PIRiB36938
RefSeqiNP_414995.1, NC_000913.3
WP_001132469.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IWGX-ray3.50A1-1049[»]
1OY6X-ray3.68A1-1049[»]
1OY8X-ray3.63A1-1049[»]
1OY9X-ray3.80A1-1049[»]
1OYDX-ray3.80A1-1049[»]
1OYEX-ray3.48A1-1049[»]
1T9TX-ray3.23A1-1049[»]
1T9UX-ray3.11A1-1049[»]
1T9VX-ray3.80A1-1049[»]
1T9WX-ray3.23A1-1049[»]
1T9XX-ray3.08A1-1049[»]
1T9YX-ray3.64A1-1049[»]
2DHHX-ray2.80A/B/C1-1049[»]
2DR6X-ray3.30A/B/C1-1049[»]
2DRDX-ray3.10A/B/C1-1049[»]
2GIFX-ray2.90A/B/C1-1049[»]
2HQCX-ray3.56A1-1049[»]
2HQDX-ray3.65A1-1049[»]
2HQFX-ray3.38A1-1049[»]
2HQGX-ray3.38A1-1049[»]
2HRTX-ray3.00A/B/C/D/E/F1-1049[»]
2I6WX-ray3.10A1-1049[»]
2J8SX-ray2.54A/B/C1-1049[»]
2RDDX-ray3.50A1-1049[»]
2W1BX-ray3.85A1-1049[»]
3AOAX-ray3.35A/B/C1-1049[»]
3AOBX-ray3.35A/B/C1-1049[»]
3AOCX-ray3.34A/B/C1-1049[»]
3AODX-ray3.30A/B/C1-1049[»]
3D9BX-ray3.42A1-1049[»]
3NOCX-ray2.70A/B/C1-1049[»]
3NOGX-ray3.34A/B/C1-1049[»]
3W9HX-ray3.05A/B/C1-1033[»]
4C48X-ray3.30A1-1047[»]
4CDIX-ray3.70A1-1049[»]
4DX5X-ray1.90A/B/C1-1049[»]
4DX6X-ray2.90A/B/C1-1049[»]
4DX7X-ray2.25A/B/C1-1049[»]
4K7QX-ray3.50A1-1049[»]
4U8VX-ray2.30A/B/C1-1049[»]
4U8YX-ray2.10A/B/C1-1049[»]
4U95X-ray2.00A/B/C1-1049[»]
4U96X-ray2.20A/B/C1-1049[»]
4ZITX-ray3.30A/B/C/D/E/F1-1049[»]
4ZIVX-ray3.16A/B/C/D/E/F1-1049[»]
4ZIWX-ray3.40A/B/C/D/E/F1-1049[»]
4ZJLX-ray3.47A/B/C/D/E/F1-1049[»]
4ZJOX-ray3.60A/B/C/D/E/F1-1049[»]
4ZJQX-ray3.59A/B/C/D/E/F1-1049[»]
4ZLJX-ray3.26A1-1049[»]
4ZLLX-ray3.36A1-1049[»]
4ZLNX-ray3.56A1-1049[»]
5EN5X-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENOX-ray2.20A/B/C39-329[»]
A/B/C561-869[»]
5ENPX-ray1.90A/B/C39-329[»]
A/B/C561-869[»]
5ENQX-ray1.80A/B/C39-329[»]
A/B/C561-869[»]
5ENRX-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENSX-ray2.80A/B/C39-329[»]
A/B/C561-869[»]
5ENTX-ray2.50A/B/C39-329[»]
A/B/C561-869[»]
5JMNX-ray2.50A/B/C1-1049[»]
5NC5X-ray3.20A/B/C1-1049[»]
5NG5electron microscopy6.50J/K/L1-1049[»]
5O66electron microscopy5.90J/K/L1-1049[»]
5V5Selectron microscopy6.50J/K/L1-1049[»]
5YILX-ray3.00A/B/C1-1049[»]
ProteinModelPortaliP31224
SMRiP31224
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259859, 386 interactors
DIPiDIP-9049N
IntActiP31224, 9 interactors
MINTiP31224
STRINGi316385.ECDH10B_0418

Chemistry databases

ChEMBLiCHEMBL1681614
DrugBankiDB03619 Deoxycholic Acid
DB04209 Dequadin
DB03825 Rhodamine 6G

Protein family/group databases

TCDBi2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

Proteomic databases

EPDiP31224
PaxDbiP31224
PRIDEiP31224

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73564; AAC73564; b0462
BAE76241; BAE76241; BAE76241
GeneIDi945108
KEGGiecj:JW0451
eco:b0462
PATRICifig|1411691.4.peg.1814

Organism-specific databases

EchoBASEiEB1655
EcoGeneiEG11704 acrB

Phylogenomic databases

eggNOGiENOG4105BZS Bacteria
COG0841 LUCA
HOGENOMiHOG000158129
InParanoidiP31224
KOiK18138
PhylomeDBiP31224

Enzyme and pathway databases

BioCyciEcoCyc:ACRB-MONOMER
MetaCyc:ACRB-MONOMER

Miscellaneous databases

EvolutionaryTraceiP31224
PROiPR:P31224

Family and domain databases

Gene3Di3.30.2090.10, 2 hits
InterProiView protein in InterPro
IPR027463 AcrB_DN_DC_subdom
IPR001036 Acrflvin-R
IPR004764 HAE1
PANTHERiPTHR32063 PTHR32063, 1 hit
PfamiView protein in Pfam
PF00873 ACR_tran, 1 hit
PRINTSiPR00702 ACRIFLAVINRP
SUPFAMiSSF82714 SSF82714, 2 hits
TIGRFAMsiTIGR00915 2A0602, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiACRB_ECOLI
AccessioniPrimary (citable) accession number: P31224
Secondary accession number(s): Q2MBW5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 7, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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