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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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 25MNKNR…ALTGC → MKKTAIAIAVALAGFATVAQ A: Fully functional (replaces endogenous signal and lipid anchor with periplasmic signal for OmpA). Add BLAST25
Mutagenesisi223 – 224FL → MM: Wild-type resistance to efflux substrates. Protein unstable; when associated with 287-M-M-288. 1 Publication2
Mutagenesisi287 – 288LL → MM: Wild-type resistance to efflux substrates. Protein unstable; when associated with 223-M-M-224. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000001868725 – 397Multidrug efflux pump subunit AcrAAdd BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi25N-palmitoyl cysteine1 Publication1
Lipidationi25S-diacylglycerol cysteineCurated1

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi55 – 61Combined sources7
Beta strandi63 – 68Combined sources6
Beta strandi74 – 79Combined sources6
Beta strandi93 – 96Combined sources4
Helixi99 – 130Combined sources32
Turni131 – 134Combined sources4
Helixi140 – 172Combined sources33
Beta strandi182 – 184Combined sources3
Beta strandi203 – 208Combined sources6
Beta strandi210 – 219Combined sources10
Turni220 – 222Combined sources3
Helixi224 – 230Combined sources7
Beta strandi244 – 247Combined sources4
Beta strandi249 – 251Combined sources3
Beta strandi258 – 263Combined sources6
Beta strandi269 – 271Combined sources3
Beta strandi273 – 280Combined sources8
Beta strandi292 – 297Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AE06.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 397Interaction with AcrBAdd BLAST226
Regioni313 – 397Required for growth on efflux drugsAdd BLAST85

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili98 – 172Add BLAST75

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG4105C1P. Bacteria.
ENOG410XNVN. LUCA.
HOGENOMiHOG000158247.
InParanoidiP0AE06.
KOiK03585.
OMAiNKNRRLT.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F1MX-ray2.71A/B/C/D45-312[»]
ProteinModelPortaliP0AE06.
SMRiP0AE06.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259860. 387 interactors.
DIPiDIP-29039N.
IntActiP0AE06. 5 interactors.
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.
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...

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: November 2, 2016
This is version 101 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.