SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P31224

- ACRB_ECOLI

UniProt

P31224 - ACRB_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Multidrug efflux pump subunit AcrB
Gene
acrB, acrE, b0462, JW0451
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - 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

GO - Molecular functioni

  1. drug transmembrane transporter activity Source: EcoCyc
  2. drug:proton antiporter 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
Complete GO annotation...

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; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic1 Publication
Transmembranei10 – 2819Helical; Name=1
Add
BLAST
Topological domaini29 – 336308Periplasmic1 Publication
Add
BLAST
Transmembranei337 – 35620Helical; Name=2
Add
BLAST
Topological domaini357 – 3659Cytoplasmic1 Publication
Transmembranei366 – 38520Helical; Name=3
Add
BLAST
Topological domaini386 – 3916Periplasmic1 Publication
Transmembranei392 – 41322Helical; Name=4
Add
BLAST
Topological domaini414 – 43825Cytoplasmic1 Publication
Add
BLAST
Transmembranei439 – 45719Helical; Name=5
Add
BLAST
Topological domaini458 – 4658Periplasmic1 Publication
Transmembranei466 – 49025Helical; Name=6
Add
BLAST
Topological domaini491 – 53848Cytoplasmic1 Publication
Add
BLAST
Transmembranei539 – 55517Helical; Name=7
Add
BLAST
Topological domaini556 – 871316Periplasmic1 Publication
Add
BLAST
Transmembranei872 – 88817Helical; Name=8
Add
BLAST
Topological domaini889 – 89810Cytoplasmic1 Publication
Transmembranei899 – 91820Helical; Name=9
Add
BLAST
Topological domaini919 – 9246Periplasmic1 Publication
Transmembranei925 – 94319Helical; Name=10
Add
BLAST
Topological domaini944 – 97229Cytoplasmic1 Publication
Add
BLAST
Transmembranei973 – 99220Helical; Name=11
Add
BLAST
Topological domaini993 – 9986Periplasmic1 Publication
Transmembranei999 – 101820Helical; Name=12
Add
BLAST
Topological domaini1019 – 104931Cytoplasmic1 Publication
Add
BLAST

GO - Cellular componenti

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

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 AcrB
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP31224.

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.
DrugBanki DB00537. Ciprofloxacin.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

Similar proteinsi