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P31224 (ACRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acriflavine resistance protein B
Gene names
Name:acrB
Synonyms:acrE
Ordered Locus Names:b0462, JW0451
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length1049 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AcrAB is a drug efflux protein with a broad substrate specificity. Ref.12 Ref.13 Ref.14

Subunit structure

Trimer. Each monomer interacts with AcrA and TolC. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.8.

Sequence similarities

Belongs to the AcrB/AcrD/AcrF (TC 2.A.6) family. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ybhTP0AAW94EBI-551006,EBI-6313593

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10491049Acriflavine resistance protein B
PRO_0000161811

Regions

Topological domain1 – 99Cytoplasmic Ref.9
Transmembrane10 – 2819Helical; Name=1
Topological domain29 – 336308Periplasmic Ref.9
Transmembrane337 – 35620Helical; Name=2
Topological domain357 – 3659Cytoplasmic Ref.9
Transmembrane366 – 38520Helical; Name=3
Topological domain386 – 3916Periplasmic Ref.9
Transmembrane392 – 41322Helical; Name=4
Topological domain414 – 43825Cytoplasmic Ref.9
Transmembrane439 – 45719Helical; Name=5
Topological domain458 – 4658Periplasmic Ref.9
Transmembrane466 – 49025Helical; Name=6
Topological domain491 – 53848Cytoplasmic Ref.9
Transmembrane539 – 55517Helical; Name=7
Topological domain556 – 871316Periplasmic Ref.9
Transmembrane872 – 88817Helical; Name=8
Topological domain889 – 89810Cytoplasmic Ref.9
Transmembrane899 – 91820Helical; Name=9
Topological domain919 – 9246Periplasmic Ref.9
Transmembrane925 – 94319Helical; Name=10
Topological domain944 – 97229Cytoplasmic Ref.9
Transmembrane973 – 99220Helical; Name=11
Topological domain993 – 9986Periplasmic Ref.9
Transmembrane999 – 101820Helical; Name=12
Topological domain1019 – 104931Cytoplasmic Ref.9

Secondary structure

1 ........................................................................................................................................................................... 1049
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31224 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 19670E3C4CC29055

FASTA1,049113,574
        10         20         30         40         50         60 
MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP GADAKTVQDT 

        70         80         90        100        110        120 
VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA DIAQVQVQNK LQLAMPLLPQ 

       130        140        150        160        170        180 
EVQQQGVSVE KSSSSFLMVV GVINTDGTMT QEDISDYVAA NMKDAISRTS GVGDVQLFGS 

       190        200        210        220        230        240 
QYAMRIWMNP NELNKFQLTP VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL 

       250        260        270        280        290        300 
TSTEEFGKIL LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL 

       310        320        330        340        350        360 
DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL VFLVMYLFLQ 

       370        380        390        400        410        420 
NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM 

       430        440        450        460        470        480 
AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS AVFVPMAFFG GSTGAIYRQF SITIVSAMAL 

       490        500        510        520        530        540 
SVLVALILTP ALCATMLKPI AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR 

       550        560        570        580        590        600 
YLVLYLIIVV GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT 

       610        620        630        640        650        660 
KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR ATRAFSQIKD 

       670        680        690        700        710        720 
AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN QLLAEAAKHP DMLTSVRPNG 

       730        740        750        760        770        780 
LEDTPQFKID IDQEKAQALG VSINDINTTL GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR 

       790        800        810        820        830        840 
MLPDDIGDWY VRAADGQMVP FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA 

       850        860        870        880        890        900 
MELMEQLASK LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS 

       910        920        930        940        950        960 
VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK DLMDKEGKGL 

       970        980        990       1000       1010       1020 
IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ NAVGTGVMGG MVTATVLAIF 

      1030       1040 
FVPVFFVVVR RRFSRKNEDI EHSHTVDHH

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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.
[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: INTERACTION WITH ACRA.
[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: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[9]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[10]"Crystal structure of bacterial multidrug efflux transporter AcrB."
Murakami S., Nakashima R., Yamashita E., Yamaguchi A.
Nature 419:587-593(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT.
[11]"Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump."
Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., Koshland D.E. Jr.
Science 300:976-980(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, SUBUNIT.
[12]"Crystal structures of a multidrug transporter reveal a functionally rotating mechanism."
Murakami S., Nakashima R., Yamashita E., Matsumoto T., Yamaguchi A.
Nature 443:173-179(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT, FUNCTION.
[13]"Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism."
Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., Pos K.M.
Science 313:1295-1298(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, FUNCTION.
[14]"Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors."
Sennhauser G., Amstutz P., Briand C., Storchenegger O., Gruetter M.G.
PLoS Biol. 5:107-113(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M94248 Genomic DNA. Translation: AAA23411.1.
U00734 Genomic DNA. Translation: AAA67135.1.
U82664 Genomic DNA. Translation: AAB40216.1.
U00096 Genomic DNA. Translation: AAC73564.1.
AP009048 Genomic DNA. Translation: BAE76241.1.
PIRB36938.
RefSeqNP_414995.1. NC_000913.2.
YP_488753.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWGX-ray3.50A1-1049[»]
1OY6X-ray3.68A1-1049[»]
1OY8X-ray3.63A1-1049[»]
1OY9X-ray3.80A1-1049[»]
1OYDX-ray3.80A1-1049[»]
1OYEX-ray3.48A1-1049[»]
1T9TX-ray3.23A1-1049[»]
1T9UX-ray3.11A1-1049[»]
1T9VX-ray3.80A1-1049[»]
1T9WX-ray3.23A1-1049[»]
1T9XX-ray3.08A1-1049[»]
1T9YX-ray3.64A1-1049[»]
2DHHX-ray2.80A/B/C1-1049[»]
2DR6X-ray3.30A/B/C1-1049[»]
2DRDX-ray3.10A/B/C1-1049[»]
2GIFX-ray2.90A/B/C1-1049[»]
2HQCX-ray3.56A1-1049[»]
2HQDX-ray3.65A1-1049[»]
2HQFX-ray3.38A1-1049[»]
2HQGX-ray3.38A1-1049[»]
2HRTX-ray3.00A/B/C/D/E/F1-1049[»]
2I6WX-ray3.10A1-1049[»]
2J8SX-ray2.54A/B/C1-1049[»]
2RDDX-ray3.50A1-1049[»]
2W1BX-ray3.85A1-1049[»]
3AOAX-ray3.35A/B/C1-1049[»]
3AOBX-ray3.35A/B/C1-1049[»]
3AOCX-ray3.34A/B/C1-1049[»]
3AODX-ray3.30A/B/C1-1049[»]
3D9BX-ray3.42A1-1049[»]
3NOCX-ray2.70A/B/C1-1049[»]
3NOGX-ray3.34A/B/C1-1049[»]
4DX5X-ray1.90A/B/C1-1049[»]
4DX6X-ray2.90A/B/C1-1049[»]
4DX7X-ray2.25A/B/C1-1049[»]
ProteinModelPortalP31224.
SMRP31224. Positions 1-1044.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9049N.
IntActP31224. 8 interactions.
MINTMINT-1286285.
STRING511145.b0462.

Protein family/group databases

TCDB2.A.6.2.2. resistance-nodulation-cell division (RND) superfamily.

Proteomic databases

PaxDbP31224.
PRIDEP31224.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73564; AAC73564; b0462.
BAE76241; BAE76241; BAE76241.
GeneID12930865.
945108.
KEGGecj:Y75_p0449.
eco:b0462.
PATRIC32116077. VBIEscCol129921_0480.

Organism-specific databases

EchoBASEEB1655.
EcoGeneEG11704. acrB.

Phylogenomic databases

eggNOGCOG0841.
HOGENOMHOG000158129.
KOK03296.
OMARMFDKST.
ProtClustDBPRK15127.

Enzyme and pathway databases

BioCycEcoCyc:ACRB-MONOMER.
ECOL316407:JW0451-MONOMER.

Gene expression databases

GenevestigatorP31224.

Family and domain databases

InterProIPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
PfamPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSPR00702. ACRIFLAVINRP.
TIGRFAMsTIGR00915. 2A0602. 1 hit.
ProtoNetSearch...

Other

BindingDBP31224.
ChEMBLCHEMBL1681614.
DrugBankDB00537. Ciprofloxacin.
EvolutionaryTraceP31224.

Entry information

Entry nameACRB_ECOLI
AccessionPrimary (citable) accession number: P31224
Secondary accession number(s): Q2MBW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents