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Protein

Multidrug efflux pump subunit AcrA

Gene

acrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.1 Publication

GO - Molecular functioni

  • drug transmembrane transporter activity Source: EcoliWiki
  • identical protein binding Source: IntAct

GO - Biological processi

  • bile acid and bile salt transport Source: EcoCyc
  • drug transmembrane transport Source: EcoCyc
  • response to antibiotic Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11703-MONOMER.
ECOL316407:JW0452-MONOMER.

Protein family/group databases

TCDBi8.A.1.6.1. the membrane fusion protein (mfp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug efflux pump subunit AcrA
Alternative name(s):
AcrAB-TolC multidrug efflux pump subunit AcrA
Acridine resistance protein A
Gene namesi
Name:acrA
Synonyms:lir, mtcA
Ordered Locus Names:b0463, JW0452
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11703. acrA.

Subcellular locationi

GO - Cellular componenti

  • intrinsic component of plasma membrane Source: GO_Central
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cannot grow on efflux substrates novobiocin or fusidic acid.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 2525MNKNR…ALTGC → MKKTAIAIAVALAGFATVAQ A: Fully functional (replaces endogenous signal and lipid anchor with periplasmic signal for OmpA). Add
BLAST
Mutagenesisi223 – 2242FL → MM: Wild-type resistance to efflux substrates. Protein unstable; when associated with 287-M-M-288. 1 Publication
Mutagenesisi287 – 2882LL → MM: Wild-type resistance to efflux substrates. Protein unstable; when associated with 223-M-M-224. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 397373Multidrug efflux pump subunit AcrAPRO_0000018687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi25 – 251N-palmitoyl cysteine1 Publication
Lipidationi25 – 251S-diacylglycerol cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiP0AE06.
PaxDbiP0AE06.
PRIDEiP0AE06.

Interactioni

Subunit structurei

Monomeric in solution. Homotrimeric; interacts indpendently with AcrB and TolC as well as AcrZ. Part of the AcrA-AcrB-TolC efflux pump. Complex assembly is independent of an efflux substrate and appears to be constitutive.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-875601,EBI-875601

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259860. 387 interactions.
DIPiDIP-29039N.
IntActiP0AE06. 5 interactions.
STRINGi511145.b0463.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 617Combined sources
Beta strandi63 – 686Combined sources
Beta strandi74 – 796Combined sources
Beta strandi93 – 964Combined sources
Helixi99 – 13032Combined sources
Turni131 – 1344Combined sources
Helixi140 – 17233Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi210 – 21910Combined sources
Turni220 – 2223Combined sources
Helixi224 – 2307Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi273 – 2808Combined sources
Beta strandi292 – 2976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F1MX-ray2.71A/B/C/D45-312[»]
ProteinModelPortaliP0AE06.
SMRiP0AE06. Positions 38-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE06.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 397226Interacts with AcrBAdd
BLAST
Regioni313 – 39785Required for growth on efflux drugsAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili98 – 17275Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG4105C1P. Bacteria.
ENOG410XNVN. LUCA.
HOGENOMiHOG000158247.
InParanoidiP0AE06.
KOiK03585.
OMAiNKNRRLT.
OrthoDBiEOG6GJBSS.
PhylomeDBiP0AE06.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL
60 70 80 90 100
QITTELPGRT SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT
110 120 130 140 150
YQATYDSAKG DLAKAQAAAN IAQLTVNRYQ KLLGTQYISK QEYDQALADA
160 170 180 190 200
QQANAAVTAA KAAVETARIN LAYTKVTSPI SGRIGKSNVT EGALVQNGQA
210 220 230 240 250
TALATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG KAKVSLITSD
260 270 280 290 300
GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG
310 320 330 340 350
LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT
360 370 380 390
EGLKAGDRVV ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS
Length:397
Mass (Da):42,197
Last modified:December 6, 2005 - v1
Checksum:i5B81DD5BC2B0A077
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00734 Genomic DNA. Translation: AAA67134.1.
M94248 Genomic DNA. Translation: AAA23410.1.
U82664 Genomic DNA. Translation: AAB40217.1.
U00096 Genomic DNA. Translation: AAC73565.1.
AP009048 Genomic DNA. Translation: BAE76242.1.
PIRiA36938.
RefSeqiNP_414996.1. NC_000913.3.
WP_001295324.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73565; AAC73565; b0463.
BAE76242; BAE76242; BAE76242.
GeneIDi945112.
KEGGiecj:JW0452.
eco:b0463.
PATRICi32116079. VBIEscCol129921_0481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00734 Genomic DNA. Translation: AAA67134.1.
M94248 Genomic DNA. Translation: AAA23410.1.
U82664 Genomic DNA. Translation: AAB40217.1.
U00096 Genomic DNA. Translation: AAC73565.1.
AP009048 Genomic DNA. Translation: BAE76242.1.
PIRiA36938.
RefSeqiNP_414996.1. NC_000913.3.
WP_001295324.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F1MX-ray2.71A/B/C/D45-312[»]
ProteinModelPortaliP0AE06.
SMRiP0AE06. Positions 38-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259860. 387 interactions.
DIPiDIP-29039N.
IntActiP0AE06. 5 interactions.
STRINGi511145.b0463.

Protein family/group databases

TCDBi8.A.1.6.1. the membrane fusion protein (mfp) family.

Proteomic databases

EPDiP0AE06.
PaxDbiP0AE06.
PRIDEiP0AE06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73565; AAC73565; b0463.
BAE76242; BAE76242; BAE76242.
GeneIDi945112.
KEGGiecj:JW0452.
eco:b0463.
PATRICi32116079. VBIEscCol129921_0481.

Organism-specific databases

EchoBASEiEB1654.
EcoGeneiEG11703. acrA.

Phylogenomic databases

eggNOGiENOG4105C1P. Bacteria.
ENOG410XNVN. LUCA.
HOGENOMiHOG000158247.
InParanoidiP0AE06.
KOiK03585.
OMAiNKNRRLT.
OrthoDBiEOG6GJBSS.
PhylomeDBiP0AE06.

Enzyme and pathway databases

BioCyciEcoCyc:EG11703-MONOMER.
ECOL316407:JW0452-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AE06.
PROiP0AE06.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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.
  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. "AcrA is a highly asymmetric protein capable of spanning the periplasm."
    Zgurskaya H.I., Nikaido H.
    J. Mol. Biol. 285:409-420(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EFFLUX, SUBUNIT, PALMITOYLATION, DISRUPTION PHENOTYPE.
  8. "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: PROTEOLYTIC PROCESSING, INTERACTION WITH ACRB.
  9. "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 ACRB AND TOLC, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  10. Cited for: HOMOTRIMERIZATION, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  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: SUBUNIT.
    Strain: K12 / MG1655 / ATCC 47076.
  12. "Conformational flexibility in the multidrug efflux system protein AcrA."
    Mikolosko J., Bobyk K., Zgurskaya H.I., Ghosh P.
    Structure 14:577-587(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 45-312, MUTAGENESIS OF 223-MET-MET-224 AND 287-LEU-LEU-288.
    Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.

Entry informationi

Entry nameiACRA_ECOLI
AccessioniPrimary (citable) accession number: P0AE06
Secondary accession number(s): P31223, Q2MBW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: March 16, 2016
This is version 98 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.