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P31224

- ACRB_ECOLI

UniProt

P31224 - ACRB_ECOLI

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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

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

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 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic1 Publication
Transmembranei10 – 2819Helical; Name=1Add
BLAST
Topological domaini29 – 336308Periplasmic1 PublicationAdd
BLAST
Transmembranei337 – 35620Helical; Name=2Add
BLAST
Topological domaini357 – 3659Cytoplasmic1 Publication
Transmembranei366 – 38520Helical; Name=3Add
BLAST
Topological domaini386 – 3916Periplasmic1 Publication
Transmembranei392 – 41322Helical; Name=4Add
BLAST
Topological domaini414 – 43825Cytoplasmic1 PublicationAdd
BLAST
Transmembranei439 – 45719Helical; Name=5Add
BLAST
Topological domaini458 – 4658Periplasmic1 Publication
Transmembranei466 – 49025Helical; Name=6Add
BLAST
Topological domaini491 – 53848Cytoplasmic1 PublicationAdd
BLAST
Transmembranei539 – 55517Helical; Name=7Add
BLAST
Topological domaini556 – 871316Periplasmic1 PublicationAdd
BLAST
Transmembranei872 – 88817Helical; Name=8Add
BLAST
Topological domaini889 – 89810Cytoplasmic1 Publication
Transmembranei899 – 91820Helical; Name=9Add
BLAST
Topological domaini919 – 9246Periplasmic1 Publication
Transmembranei925 – 94319Helical; Name=10Add
BLAST
Topological domaini944 – 97229Cytoplasmic1 PublicationAdd
BLAST
Transmembranei973 – 99220Helical; Name=11Add
BLAST
Topological domaini993 – 9986Periplasmic1 Publication
Transmembranei999 – 101820Helical; Name=12Add
BLAST
Topological domaini1019 – 104931Cytoplasmic1 PublicationAdd
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 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 – 65Combined sources
Helixi9 – 2921Combined sources
Beta strandi32 – 354Combined sources
Beta strandi42 – 487Combined sources
Helixi54 – 607Combined sources
Helixi62 – 676Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 949Combined sources
Beta strandi95 – 973Combined sources
Helixi100 – 11415Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 1256Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi137 – 1448Combined sources
Beta strandi145 – 1473Combined sources
Helixi151 – 16111Combined sources
Helixi163 – 1675Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi172 – 1798Combined sources
Beta strandi182 – 1887Combined sources
Helixi190 – 1956Combined sources
Helixi200 – 21011Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi232 – 2354Combined sources
Helixi243 – 2475Combined sources
Beta strandi250 – 2534Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2613Combined sources
Helixi262 – 2643Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi278 – 2814Combined sources
Beta strandi284 – 29411Combined sources
Beta strandi295 – 2984Combined sources
Helixi299 – 31315Combined sources
Helixi314 – 3163Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi321 – 3299Combined sources
Helixi330 – 35930Combined sources
Helixi362 – 38524Combined sources
Helixi392 – 42332Combined sources
Helixi427 – 45327Combined sources
Helixi455 – 4584Combined sources
Helixi461 – 49636Combined sources
Turni505 – 5084Combined sources
Helixi512 – 53625Combined sources
Beta strandi537 – 5393Combined sources
Helixi540 – 55819Combined sources
Beta strandi561 – 5644Combined sources
Beta strandi570 – 5778Combined sources
Helixi584 – 60118Combined sources
Turni603 – 6053Combined sources
Beta strandi606 – 6149Combined sources
Beta strandi617 – 6193Combined sources
Beta strandi621 – 6233Combined sources
Beta strandi624 – 6318Combined sources
Helixi634 – 6363Combined sources
Helixi640 – 6423Combined sources
Helixi644 – 65512Combined sources
Beta strandi658 – 6603Combined sources
Beta strandi662 – 6665Combined sources
Helixi672 – 6743Combined sources
Beta strandi677 – 68610Combined sources
Helixi692 – 70615Combined sources
Turni710 – 7123Combined sources
Beta strandi713 – 7208Combined sources
Beta strandi724 – 7318Combined sources
Helixi733 – 7397Combined sources
Helixi743 – 75513Combined sources
Beta strandi757 – 7648Combined sources
Beta strandi767 – 7759Combined sources
Helixi777 – 7793Combined sources
Beta strandi780 – 7823Combined sources
Helixi783 – 7886Combined sources
Beta strandi790 – 7923Combined sources
Beta strandi794 – 7963Combined sources
Beta strandi798 – 8003Combined sources
Helixi801 – 8033Combined sources
Beta strandi805 – 8128Combined sources
Beta strandi814 – 8196Combined sources
Beta strandi822 – 83110Combined sources
Beta strandi833 – 8353Combined sources
Helixi837 – 84913Combined sources
Beta strandi855 – 8595Combined sources
Helixi861 – 8644Combined sources
Beta strandi865 – 8684Combined sources
Turni869 – 8713Combined sources
Helixi873 – 89220Combined sources
Beta strandi895 – 8973Combined sources
Helixi898 – 9025Combined sources
Helixi905 – 91915Combined sources
Helixi925 – 95430Combined sources
Turni955 – 9573Combined sources
Helixi960 – 98526Combined sources
Helixi987 – 9904Combined sources
Beta strandi994 – 9963Combined sources
Helixi997 – 103236Combined sources
Turni1033 – 10353Combined sources
Beta strandi1039 – 10413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRiP31224. Positions 1-1044.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31224.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0841.
HOGENOMiHOG000158129.
InParanoidiP31224.
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

        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.
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:
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 .
PIRi B36938.
RefSeqi NP_414995.1. NC_000913.3.
YP_488753.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRi P31224. Positions 1-1044.
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.
InParanoidi P31224.
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: November 26, 2014
This is version 142 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