P0AE06 (ACRA_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acriflavine resistance protein A | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 397 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | AcrAB is a drug efflux protein with a broad substrate specificity. |
| Subunit structure | |
| Subcellular location | |
| Sequence similarities | Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Signal |
| PTM | Lipoprotein Palmitate |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | plasma membrane Inferred from direct assay Ref.8. Source: EcoCyc |
| Molecular_function | drug transmembrane transporter activity Inferred from mutant phenotype Ref.1. Source: EcoliWiki |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | |||||||||||||||||||||||||||||||||||||||
| Chain | 25 – 397 | 373 | Acriflavine resistance protein A | PRO_0000018687 | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Lipidation | 25 | 1 | N-palmitoyl cysteine Potential | ||||||||||||||||||||||||||||||||||||||
| Lipidation | 25 | 1 | S-diacylglycerol cysteine Potential | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 61 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 63 – 68 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 79 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 93 – 96 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 99 – 130 | 32 | |||||||||||||||||||||||||||||||||||||||
| Turn | 131 – 134 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 140 – 172 | 33 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 182 – 184 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 203 – 208 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 210 – 219 | 10 | |||||||||||||||||||||||||||||||||||||||
| Turn | 220 – 222 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 244 – 247 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 249 – 251 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 258 – 263 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 269 – 271 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 273 – 280 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 292 – 297 | 6 | |||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [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] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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: PROTEOLYTIC PROCESSING, INTERACTION WITH ACRB. |
| [8] | "Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract] Cited for: HOMOTRIMERIZATION, SUBCELLULAR LOCATION. Strain: BL21-DE3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||
| PIR | A36938. | ||||||||||||
| RefSeq | NP_414996.1. NC_000913.2. YP_488754.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P0AE06. | ||||||||||||
| SMR | P0AE06. Positions 38-374. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-29039N. | ||||||||||||
| IntAct | P0AE06. 3 interactions. | ||||||||||||
| STRING | 511145.b0463. | ||||||||||||
Protein family/group databases | |||||||||||||
| TCDB | 8.A.1.6.1. membrane fusion protein (MFP) family. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P0AE06. | ||||||||||||
| PRIDE | P0AE06. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC73565; AAC73565; b0463. BAE76242; BAE76242; BAE76242. | ||||||||||||
| GeneID | 12930866. 945112. | ||||||||||||
| KEGG | ecj:Y75_p0450. eco:b0463. | ||||||||||||
| PATRIC | 32116079. VBIEscCol129921_0481. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB1654. | ||||||||||||
| EcoGene | EG11703. acrA. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0845. | ||||||||||||
| HOGENOM | HOG000158247. | ||||||||||||
| KO | K03585. | ||||||||||||
| OMA | DGLKYPQ. | ||||||||||||
| ProtClustDB | PRK15030. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG11703-MONOMER. ECOL316407:JW0452-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0AE06. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR006143. RND_pump_MFP. [Graphical view] | ||||||||||||
| Pfam | PF00529. HlyD. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR01730. RND_mfp. 1 hit. | ||||||||||||
| PROSITE | PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P0AE06. | ||||||||||||
Entry information
| Entry name | ACRA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0AE06 Secondary accession number(s): P31223, Q2MBW4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
