P31224 · ACRB_ECOLI

Function

function

AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates.
(Microbial infection) 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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentefflux pump complex
Cellular Componentmembrane
Cellular Componentperiplasmic side of plasma membrane
Cellular Componentplasma membrane
Molecular Functionalkane transmembrane transporter activity
Molecular Functionbile acid transmembrane transporter activity
Molecular Functionefflux transmembrane transporter activity
Molecular Functionenterobactin transmembrane transporter activity
Molecular Functionidentical protein binding
Molecular Functionxenobiotic transmembrane transporter activity
Biological Processalkane transport
Biological Processbile acid and bile salt transport
Biological Processenterobactin transport
Biological Processfatty acid transport
Biological Processresponse to antibiotic
Biological Processresponse to toxic substance
Biological Processresponse to xenobiotic stimulus
Biological Processxenobiotic detoxification by transmembrane export across the cell outer membrane
Biological Processxenobiotic transport

Keywords

Enzyme and pathway databases

Protein family/group databases

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

Names & Taxonomy

Protein names

  • Recommended name
    Multidrug efflux pump subunit AcrB
  • Alternative names
    • AcrAB-TolC multidrug efflux pump subunit AcrB
    • Acridine resistance protein B

Gene names

    • Name
      acrB
    • Synonyms
      acrE
    • Ordered locus names
      b0462, JW0451

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W4573
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P31224
  • Secondary accessions
    • Q2MBW5

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Cytoplasmic
Transmembrane10-28Helical; Name=1
Topological domain29-336Periplasmic
Transmembrane337-356Helical; Name=2
Topological domain357-365Cytoplasmic
Transmembrane366-385Helical; Name=3
Topological domain386-391Periplasmic
Transmembrane392-413Helical; Name=4
Topological domain414-438Cytoplasmic
Transmembrane439-457Helical; Name=5
Topological domain458-465Periplasmic
Transmembrane466-490Helical; Name=6
Topological domain491-538Cytoplasmic
Transmembrane539-555Helical; Name=7
Topological domain556-871Periplasmic
Transmembrane872-888Helical; Name=8
Topological domain889-898Cytoplasmic
Transmembrane899-918Helical; Name=9
Topological domain919-924Periplasmic
Transmembrane925-943Helical; Name=10
Topological domain944-972Cytoplasmic
Transmembrane973-992Helical; Name=11
Topological domain993-998Periplasmic
Transmembrane999-1018Helical; Name=12
Topological domain1019-1049Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

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

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis526Partially restores chloramphenicol resistance to an AcrZG30R mutant.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001618111-1049Multidrug efflux pump subunit AcrB

Proteomic databases

Expression

Induction

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

Interaction

Subunit

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.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P31224acrB P312249EBI-551006, EBI-551006
BINARY P31224acrZ P0AAW97EBI-551006, EBI-6313593
BINARY P31224yajC P0ADZ72EBI-551006, EBI-1130723
View interactors in UniProtKB
View CPX-4263 in Complex Portal

Protein-protein interaction databases

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,049
  • Mass (Da)
    113,574
  • Last updated
    1993-07-01 v1
  • Checksum
    19670E3C4CC29055
MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGRYLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M94248
EMBL· GenBank· DDBJ
AAA23411.1
EMBL· GenBank· DDBJ
Genomic DNA
U00734
EMBL· GenBank· DDBJ
AAA67135.1
EMBL· GenBank· DDBJ
Genomic DNA
U82664
EMBL· GenBank· DDBJ
AAB40216.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC73564.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE76241.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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