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P31224

- ACRB_ECOLI

UniProt

P31224 - ACRB_ECOLI

Protein

Multidrug efflux pump subunit AcrB

Gene

acrB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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

    GO - Molecular functioni

    1. drug:proton antiporter activity Source: EcoCyc
    2. drug transmembrane transporter activity Source: EcoCyc
    3. protein binding Source: IntAct

    GO - Biological processi

    1. drug export Source: GOC
    2. drug transmembrane transport Source: EcoCyc
    3. response to drug Source: EcoCyc

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:ACRB-MONOMER.
    ECOL316407:JW0451-MONOMER.
    RETL1328306-WGS:GSTH-3471-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11704. acrB.

    Subcellular locationi

    Cell inner membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. integral component of plasma membrane Source: EcoCyc
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi526 – 5261H → Y: Partially restores chloramphenicol resistance to an AcrZ G30R mutant. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10491049Multidrug efflux pump subunit AcrBPRO_0000161811Add
    BLAST

    Proteomic databases

    PaxDbiP31224.
    PRIDEiP31224.

    Expressioni

    Inductioni

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

    Gene expression databases

    GenevestigatoriP31224.

    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

    WithEntry#Exp.IntActNotes
    acrZP0AAW94EBI-551006,EBI-6313593

    Protein-protein interaction databases

    DIPiDIP-9049N.
    IntActiP31224. 8 interactions.
    MINTiMINT-1286285.
    STRINGi511145.b0462.

    Structurei

    Secondary structure

    1
    1049
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 65
    Helixi9 – 2921
    Beta strandi32 – 354
    Beta strandi42 – 487
    Helixi54 – 607
    Helixi62 – 676
    Beta strandi75 – 839
    Beta strandi86 – 949
    Beta strandi95 – 973
    Helixi100 – 11415
    Helixi115 – 1173
    Helixi120 – 1256
    Beta strandi128 – 1325
    Beta strandi137 – 1448
    Beta strandi145 – 1473
    Helixi151 – 16111
    Helixi163 – 1675
    Beta strandi168 – 1714
    Beta strandi172 – 1798
    Beta strandi182 – 1887
    Helixi190 – 1956
    Helixi200 – 21011
    Beta strandi215 – 2195
    Beta strandi232 – 2354
    Helixi243 – 2475
    Beta strandi250 – 2534
    Turni255 – 2573
    Beta strandi259 – 2613
    Helixi262 – 2643
    Beta strandi266 – 2738
    Beta strandi278 – 2814
    Beta strandi284 – 29411
    Beta strandi295 – 2984
    Helixi299 – 31315
    Helixi314 – 3163
    Beta strandi317 – 3193
    Beta strandi321 – 3299
    Helixi330 – 35930
    Helixi362 – 38524
    Helixi392 – 42332
    Helixi427 – 45327
    Helixi455 – 4584
    Helixi461 – 49636
    Turni505 – 5084
    Helixi512 – 53625
    Beta strandi537 – 5393
    Helixi540 – 55819
    Beta strandi561 – 5644
    Beta strandi570 – 5778
    Helixi584 – 60118
    Turni603 – 6053
    Beta strandi606 – 6149
    Beta strandi617 – 6193
    Beta strandi621 – 6233
    Beta strandi624 – 6318
    Helixi634 – 6363
    Helixi640 – 6423
    Helixi644 – 65512
    Beta strandi658 – 6603
    Beta strandi662 – 6665
    Helixi672 – 6743
    Beta strandi677 – 68610
    Helixi692 – 70615
    Turni710 – 7123
    Beta strandi713 – 7208
    Beta strandi724 – 7318
    Helixi733 – 7397
    Helixi743 – 75513
    Beta strandi757 – 7648
    Beta strandi767 – 7759
    Helixi777 – 7793
    Beta strandi780 – 7823
    Helixi783 – 7886
    Beta strandi790 – 7923
    Beta strandi794 – 7963
    Beta strandi798 – 8003
    Helixi801 – 8033
    Beta strandi805 – 8128
    Beta strandi814 – 8196
    Beta strandi822 – 83110
    Beta strandi833 – 8353
    Helixi837 – 84913
    Beta strandi855 – 8595
    Helixi861 – 8644
    Beta strandi865 – 8684
    Turni869 – 8713
    Helixi873 – 89220
    Beta strandi895 – 8973
    Helixi898 – 9025
    Helixi905 – 91915
    Helixi925 – 95430
    Turni955 – 9573
    Helixi960 – 98526
    Helixi987 – 9904
    Beta strandi994 – 9963
    Helixi997 – 103236
    Turni1033 – 10353
    Beta strandi1039 – 10413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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-ray3.50A1-1036[»]
    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[»]
    ProteinModelPortaliP31224.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31224.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99Cytoplasmic1 Publication
    Topological domaini29 – 336308Periplasmic1 PublicationAdd
    BLAST
    Topological domaini357 – 3659Cytoplasmic1 Publication
    Topological domaini386 – 3916Periplasmic1 Publication
    Topological domaini414 – 43825Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini458 – 4658Periplasmic1 Publication
    Topological domaini491 – 53848Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini556 – 871316Periplasmic1 PublicationAdd
    BLAST
    Topological domaini889 – 89810Cytoplasmic1 Publication
    Topological domaini919 – 9246Periplasmic1 Publication
    Topological domaini944 – 97229Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini993 – 9986Periplasmic1 Publication
    Topological domaini1019 – 104931Cytoplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 2819Helical; Name=1Add
    BLAST
    Transmembranei337 – 35620Helical; Name=2Add
    BLAST
    Transmembranei366 – 38520Helical; Name=3Add
    BLAST
    Transmembranei392 – 41322Helical; Name=4Add
    BLAST
    Transmembranei439 – 45719Helical; Name=5Add
    BLAST
    Transmembranei466 – 49025Helical; Name=6Add
    BLAST
    Transmembranei539 – 55517Helical; Name=7Add
    BLAST
    Transmembranei872 – 88817Helical; Name=8Add
    BLAST
    Transmembranei899 – 91820Helical; Name=9Add
    BLAST
    Transmembranei925 – 94319Helical; Name=10Add
    BLAST
    Transmembranei973 – 99220Helical; Name=11Add
    BLAST
    Transmembranei999 – 101820Helical; Name=12Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0841.
    HOGENOMiHOG000158129.
    KOiK18138.
    OMAiQFKINID.
    OrthoDBiEOG683S5M.
    PhylomeDBiP31224.

    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.

    P31224-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP     50
    GADAKTVQDT VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA 100
    DIAQVQVQNK LQLAMPLLPQ EVQQQGVSVE KSSSSFLMVV GVINTDGTMT 150
    QEDISDYVAA NMKDAISRTS GVGDVQLFGS QYAMRIWMNP NELNKFQLTP 200
    VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL TSTEEFGKIL 250
    LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL 300
    DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL 350
    VFLVMYLFLQ NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL 400
    AIGLLVDDAI VVVENVERVM AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS 450
    AVFVPMAFFG GSTGAIYRQF SITIVSAMAL SVLVALILTP ALCATMLKPI 500
    AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR YLVLYLIIVV 550
    GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT 600
    KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR 650
    ATRAFSQIKD AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN 700
    QLLAEAAKHP DMLTSVRPNG LEDTPQFKID IDQEKAQALG VSINDINTTL 750
    GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR MLPDDIGDWY VRAADGQMVP 800
    FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA MELMEQLASK 850
    LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS 900
    VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK 950
    DLMDKEGKGL IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ 1000
    NAVGTGVMGG MVTATVLAIF FVPVFFVVVR RRFSRKNEDI EHSHTVDHH 1049
    Length:1,049
    Mass (Da):113,574
    Last modified:July 1, 1993 - v1
    Checksum:i19670E3C4CC29055
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488753.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73564; AAC73564; b0462.
    BAE76241; BAE76241; BAE76241.
    GeneIDi12930865.
    945108.
    KEGGiecj:Y75_p0449.
    eco:b0462.
    PATRICi32116077. VBIEscCol129921_0480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi B36938.
    RefSeqi NP_414995.1. NC_000913.3.
    YP_488753.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IWG X-ray 3.50 A 1-1049 [» ]
    1OY6 X-ray 3.68 A 1-1049 [» ]
    1OY8 X-ray 3.63 A 1-1049 [» ]
    1OY9 X-ray 3.80 A 1-1049 [» ]
    1OYD X-ray 3.80 A 1-1049 [» ]
    1OYE X-ray 3.48 A 1-1049 [» ]
    1T9T X-ray 3.23 A 1-1049 [» ]
    1T9U X-ray 3.11 A 1-1049 [» ]
    1T9V X-ray 3.80 A 1-1049 [» ]
    1T9W X-ray 3.23 A 1-1049 [» ]
    1T9X X-ray 3.08 A 1-1049 [» ]
    1T9Y X-ray 3.64 A 1-1049 [» ]
    2DHH X-ray 2.80 A/B/C 1-1049 [» ]
    2DR6 X-ray 3.30 A/B/C 1-1049 [» ]
    2DRD X-ray 3.10 A/B/C 1-1049 [» ]
    2GIF X-ray 2.90 A/B/C 1-1049 [» ]
    2HQC X-ray 3.56 A 1-1049 [» ]
    2HQD X-ray 3.65 A 1-1049 [» ]
    2HQF X-ray 3.38 A 1-1049 [» ]
    2HQG X-ray 3.38 A 1-1049 [» ]
    2HRT X-ray 3.00 A/B/C/D/E/F 1-1049 [» ]
    2I6W X-ray 3.10 A 1-1049 [» ]
    2J8S X-ray 2.54 A/B/C 1-1049 [» ]
    2RDD X-ray 3.50 A 1-1036 [» ]
    2W1B X-ray 3.85 A 1-1049 [» ]
    3AOA X-ray 3.35 A/B/C 1-1049 [» ]
    3AOB X-ray 3.35 A/B/C 1-1049 [» ]
    3AOC X-ray 3.34 A/B/C 1-1049 [» ]
    3AOD X-ray 3.30 A/B/C 1-1049 [» ]
    3D9B X-ray 3.42 A 1-1049 [» ]
    3NOC X-ray 2.70 A/B/C 1-1049 [» ]
    3NOG X-ray 3.34 A/B/C 1-1049 [» ]
    3W9H X-ray 3.05 A/B/C 1-1033 [» ]
    4C48 X-ray 3.30 A 1-1047 [» ]
    4CDI X-ray 3.70 A 1-1049 [» ]
    4DX5 X-ray 1.90 A/B/C 1-1049 [» ]
    4DX6 X-ray 2.90 A/B/C 1-1049 [» ]
    4DX7 X-ray 2.25 A/B/C 1-1049 [» ]
    4K7Q X-ray 3.50 A 1-1049 [» ]
    ProteinModelPortali P31224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9049N.
    IntActi P31224. 8 interactions.
    MINTi MINT-1286285.
    STRINGi 511145.b0462.

    Chemistry

    BindingDBi P31224.
    ChEMBLi CHEMBL1681614.

    Protein family/group databases

    TCDBi 2.A.6.2.2. the resistance-nodulation-cell division (rnd) superfamily.

    Proteomic databases

    PaxDbi P31224.
    PRIDEi P31224.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73564 ; AAC73564 ; b0462 .
    BAE76241 ; BAE76241 ; BAE76241 .
    GeneIDi 12930865.
    945108.
    KEGGi ecj:Y75_p0449.
    eco:b0462.
    PATRICi 32116077. VBIEscCol129921_0480.

    Organism-specific databases

    EchoBASEi EB1655.
    EcoGenei EG11704. acrB.

    Phylogenomic databases

    eggNOGi COG0841.
    HOGENOMi HOG000158129.
    KOi K18138.
    OMAi QFKINID.
    OrthoDBi EOG683S5M.
    PhylomeDBi P31224.

    Enzyme and pathway databases

    BioCyci EcoCyc:ACRB-MONOMER.
    ECOL316407:JW0451-MONOMER.
    RETL1328306-WGS:GSTH-3471-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P31224.
    PROi P31224.

    Gene expression databases

    Genevestigatori P31224.

    Family and domain databases

    Gene3Di 3.30.2090.10. 2 hits.
    InterProi IPR027463. AcrB_DN_DC_subdom.
    IPR001036. Acrflvin-R.
    IPR004764. HAE1.
    [Graphical view ]
    Pfami PF00873. ACR_tran. 1 hit.
    [Graphical view ]
    PRINTSi PR00702. ACRIFLAVINRP.
    SUPFAMi SSF82714. SSF82714. 2 hits.
    TIGRFAMsi TIGR00915. 2A0602. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the acrAB operon from Escherichia coli."
      Xu J., Bertrand K.P.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Molecular cloning and characterization of acrA and acrE genes of Escherichia coli."
      Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.
      J. Bacteriol. 175:6299-6313(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W4573.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli."
      Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.
      Mol. Microbiol. 16:45-55(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Molecular construction of a multidrug exporter system, AcrAB: molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA."
      Kawabe T., Fujihira E., Yamaguchi A.
      J. Biochem. 128:195-200(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACRA.
    8. "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
      Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
      Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACRA AND TOLC, SUBUNIT, SUBCELLULAR LOCATION.
      Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
    9. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    10. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: K12 / MG1655 / ATCC 47076.
    11. "Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance."
      Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G.
      Proc. Natl. Acad. Sci. U.S.A. 109:16696-16701(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACRZ, SUBUNIT, INDUCTION, MUTAGENESIS OF HIS-526.
      Strain: K12 / MG1655 / ATCC 47076.
    12. "Crystal structure of bacterial multidrug efflux transporter AcrB."
      Murakami S., Nakashima R., Yamashita E., Yamaguchi A.
      Nature 419:587-593(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT.
    13. "Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump."
      Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., Koshland D.E. Jr.
      Science 300:976-980(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, SUBUNIT.
    14. "Crystal structures of a multidrug transporter reveal a functionally rotating mechanism."
      Murakami S., Nakashima R., Yamashita E., Matsumoto T., Yamaguchi A.
      Nature 443:173-179(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT, FUNCTION.
    15. "Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism."
      Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., Pos K.M.
      Science 313:1295-1298(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, FUNCTION.
    16. "Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors."
      Sennhauser G., Amstutz P., Briand C., Storchenegger O., Gruetter M.G.
      PLoS Biol. 5:107-113(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiACRB_ECOLI
    AccessioniPrimary (citable) accession number: P31224
    Secondary accession number(s): Q2MBW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3