Acriflavine resistance protein A precursor - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P0AE06 (ACRA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acriflavine resistance protein A

Gene names

Name:	acrA
Synonyms:	lir, mtcA
Ordered Locus Names:	b0463, JW0452

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	Homotrimeric; interacts with AcrB. Ref.7 Ref.8
Subcellular location	Cell inner membrane; Lipid-anchor Ref.8.
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

Chain

25 – 397

373

Acriflavine resistance protein A

PRO_0000018687

Amino acid modifications

Lipidation

N-palmitoyl cysteine Potential

Lipidation

S-diacylglycerol cysteine Potential

Secondary structure

397

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AE06 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 5B81DD5BC2B0A077
Show »

FASTA

397

42,197

        10         20         30         40         50         60 
MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL QITTELPGRT 

        70         80         90        100        110        120 
SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT YQATYDSAKG DLAKAQAAAN 

       130        140        150        160        170        180 
IAQLTVNRYQ KLLGTQYISK QEYDQALADA QQANAAVTAA KAAVETARIN LAYTKVTSPI 

       190        200        210        220        230        240 
SGRIGKSNVT EGALVQNGQA TALATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG 

       250        260        270        280        290        300 
KAKVSLITSD GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG 

       310        320        330        340        350        360 
LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT EGLKAGDRVV 

       370        380        390 
ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS

« Hide

References

	« Hide 'large scale' referencesShow '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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F1M	X-ray	2.71	A/B/C/D	45-312	[»]

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.

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

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents