ACRB_ECOLI
ID ACRB_ECOLI Reviewed; 1049 AA.
AC P31224; Q2MBW5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Multidrug efflux pump subunit AcrB;
DE AltName: Full=AcrAB-TolC multidrug efflux pump subunit AcrB;
DE AltName: Full=Acridine resistance protein B;
GN Name=acrB; Synonyms=acrE; OrderedLocusNames=b0462, JW0451;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Xu J., Bertrand K.P.;
RT "Nucleotide sequence of the acrAB operon from Escherichia coli.";
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W4573;
RX PubMed=8407802; DOI=10.1128/jb.175.19.6299-6313.1993;
RA Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
RT "Molecular cloning and characterization of acrA and acrE genes of
RT Escherichia coli.";
RL J. Bacteriol. 175:6299-6313(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RX PubMed=7651136; DOI=10.1111/j.1365-2958.1995.tb02390.x;
RA Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
RT "Genes acrA and acrB encode a stress-induced efflux system of Escherichia
RT coli.";
RL Mol. Microbiol. 16:45-55(1995).
RN [7]
RP INTERACTION WITH ACRA.
RX PubMed=10920254; DOI=10.1093/oxfordjournals.jbchem.a022741;
RA Kawabe T., Fujihira E., Yamaguchi A.;
RT "Molecular construction of a multidrug exporter system, AcrAB: molecular
RT interaction between AcrA and AcrB, and cleavage of the N-terminal signal
RT sequence of AcrA.";
RL J. Biochem. 128:195-200(2000).
RN [8]
RP INTERACTION WITH ACRA AND TOLC, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=15228545; DOI=10.1111/j.1365-2958.2004.04158.x;
RA Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.;
RT "Interactions underlying assembly of the Escherichia coli AcrAB-TolC
RT multidrug efflux system.";
RL Mol. Microbiol. 53:697-706(2004).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=18761695; DOI=10.1111/j.1365-2958.2008.06404.x;
RA Aoki S.K., Malinverni J.C., Jacoby K., Thomas B., Pamma R., Trinh B.N.,
RA Remers S., Webb J., Braaten B.A., Silhavy T.J., Low D.A.;
RT "Contact-dependent growth inhibition requires the essential outer membrane
RT protein BamA (YaeT) as the receptor and the inner membrane transport
RT protein AcrB.";
RL Mol. Microbiol. 70:323-340(2008).
RN [12]
RP FUNCTION, INTERACTION WITH ACRZ, SUBUNIT, INDUCTION, AND MUTAGENESIS OF
RP HIS-526.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23010927; DOI=10.1073/pnas.1210093109;
RA Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G.;
RT "Conserved small protein associates with the multidrug efflux pump AcrB and
RT differentially affects antibiotic resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16696-16701(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=12374972; DOI=10.1038/nature01050;
RA Murakami S., Nakashima R., Yamashita E., Yamaguchi A.;
RT "Crystal structure of bacterial multidrug efflux transporter AcrB.";
RL Nature 419:587-593(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, AND
RP SUBUNIT.
RX PubMed=12738864; DOI=10.1126/science.1083137;
RA Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., Koshland D.E. Jr.;
RT "Structural basis of multiple drug-binding capacity of the AcrB multidrug
RT efflux pump.";
RL Science 300:976-980(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT,
RP AND FUNCTION.
RX PubMed=16915237; DOI=10.1038/nature05076;
RA Murakami S., Nakashima R., Yamashita E., Matsumoto T., Yamaguchi A.;
RT "Crystal structures of a multidrug transporter reveal a functionally
RT rotating mechanism.";
RL Nature 443:173-179(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=16946072; DOI=10.1126/science.1131542;
RA Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., Pos K.M.;
RT "Structural asymmetry of AcrB trimer suggests a peristaltic pump
RT mechanism.";
RL Science 313:1295-1298(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=17194213; DOI=10.1371/journal.pbio.0050007;
RA Sennhauser G., Amstutz P., Briand C., Storchenegger O., Gruetter M.G.;
RT "Drug export pathway of multidrug exporter AcrB revealed by DARPin
RT inhibitors.";
RL PLoS Biol. 5:107-113(2007).
CC -!- FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with
CC broad substrate specificity that uses the proton motive force to export
CC substrates. {ECO:0000269|PubMed:16915237, ECO:0000269|PubMed:16946072,
CC ECO:0000269|PubMed:17194213, ECO:0000269|PubMed:23010927}.
CC -!- FUNCTION: (Microbial infection) Involved in contact-dependent growth
CC inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its
CC role in CDI is independent of the AcrA-AcrB-TolC efflux pump complex.
CC {ECO:0000269|PubMed:18761695}.
CC -!- SUBUNIT: Homotrimer, with large domains that extend into the periplasm,
CC interacts with AcrA and TolC. AcrA may be required to stably link this
CC protein and TolC. Interacts with AcrZ. Part of the AcrA-AcrB-AcrZ-TolC
CC efflux pump. {ECO:0000269|PubMed:10920254, ECO:0000269|PubMed:12374972,
CC ECO:0000269|PubMed:12738864, ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16915237,
CC ECO:0000269|PubMed:16946072, ECO:0000269|PubMed:17194213,
CC ECO:0000269|PubMed:23010927}.
CC -!- INTERACTION:
CC P31224; P31224: acrB; NbExp=9; IntAct=EBI-551006, EBI-551006;
CC P31224; P0AAW9: acrZ; NbExp=7; IntAct=EBI-551006, EBI-6313593;
CC P31224; P0ADZ7: yajC; NbExp=2; IntAct=EBI-551006, EBI-1130723;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: Positively regulated by MarA, Rob and SoxS transcriptional
CC regulators (at protein level). {ECO:0000269|PubMed:23010927}.
CC -!- DISRUPTION PHENOTYPE: Loss of susceptibility to contact-dependent
CC growth inhibition (CDI); inhibiting cells still contact the target.
CC {ECO:0000269|PubMed:18761695}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; M94248; AAA23411.1; -; Genomic_DNA.
DR EMBL; U00734; AAA67135.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40216.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73564.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76241.1; -; Genomic_DNA.
DR PIR; B36938; B36938.
DR RefSeq; NP_414995.1; NC_000913.3.
DR RefSeq; WP_001132469.1; NZ_STEB01000007.1.
DR PDB; 1IWG; X-ray; 3.50 A; A=1-1049.
DR PDB; 1OY6; X-ray; 3.68 A; A=1-1049.
DR PDB; 1OY8; X-ray; 3.63 A; A=1-1049.
DR PDB; 1OY9; X-ray; 3.80 A; A=1-1049.
DR PDB; 1OYD; X-ray; 3.80 A; A=1-1049.
DR PDB; 1OYE; X-ray; 3.48 A; A=1-1049.
DR PDB; 1T9T; X-ray; 3.23 A; A=1-1049.
DR PDB; 1T9U; X-ray; 3.11 A; A=1-1049.
DR PDB; 1T9V; X-ray; 3.80 A; A=1-1049.
DR PDB; 1T9W; X-ray; 3.23 A; A=1-1049.
DR PDB; 1T9X; X-ray; 3.08 A; A=1-1049.
DR PDB; 1T9Y; X-ray; 3.64 A; A=1-1049.
DR PDB; 2DHH; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 2DR6; X-ray; 3.30 A; A/B/C=1-1049.
DR PDB; 2DRD; X-ray; 3.10 A; A/B/C=1-1049.
DR PDB; 2GIF; X-ray; 2.90 A; A/B/C=1-1049.
DR PDB; 2HQC; X-ray; 3.56 A; A=1-1049.
DR PDB; 2HQD; X-ray; 3.65 A; A=1-1049.
DR PDB; 2HQF; X-ray; 3.38 A; A=1-1049.
DR PDB; 2HQG; X-ray; 3.38 A; A=1-1049.
DR PDB; 2HRT; X-ray; 3.00 A; A/B/C/D/E/F=1-1049.
DR PDB; 2I6W; X-ray; 3.10 A; A=1-1049.
DR PDB; 2J8S; X-ray; 2.54 A; A/B/C=1-1049.
DR PDB; 2RDD; X-ray; 3.50 A; A=1-1049.
DR PDB; 2W1B; X-ray; 3.85 A; A=1-1049.
DR PDB; 3AOA; X-ray; 3.35 A; A/B/C=1-1049.
DR PDB; 3AOB; X-ray; 3.35 A; A/B/C=1-1049.
DR PDB; 3AOC; X-ray; 3.34 A; A/B/C=1-1049.
DR PDB; 3AOD; X-ray; 3.30 A; A/B/C=1-1049.
DR PDB; 3D9B; X-ray; 3.42 A; A=1-1049.
DR PDB; 3NOC; X-ray; 2.70 A; A/B/C=1-1049.
DR PDB; 3NOG; X-ray; 3.34 A; A/B/C=1-1049.
DR PDB; 3W9H; X-ray; 3.05 A; A/B/C=1-1033.
DR PDB; 4C48; X-ray; 3.30 A; A=1-1047.
DR PDB; 4CDI; X-ray; 3.70 A; A=1-1049.
DR PDB; 4DX5; X-ray; 1.90 A; A/B/C=1-1049.
DR PDB; 4DX6; X-ray; 2.90 A; A/B/C=1-1049.
DR PDB; 4DX7; X-ray; 2.25 A; A/B/C=1-1049.
DR PDB; 4K7Q; X-ray; 3.50 A; A=1-1049.
DR PDB; 4U8V; X-ray; 2.30 A; A/B/C=1-1049.
DR PDB; 4U8Y; X-ray; 2.10 A; A/B/C=1-1049.
DR PDB; 4U95; X-ray; 2.00 A; A/B/C=1-1049.
DR PDB; 4U96; X-ray; 2.20 A; A/B/C=1-1049.
DR PDB; 4ZIT; X-ray; 3.30 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZIV; X-ray; 3.16 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZIW; X-ray; 3.40 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZJL; X-ray; 3.47 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZJO; X-ray; 3.60 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZJQ; X-ray; 3.59 A; A/B/C/D/E/F=1-1049.
DR PDB; 4ZLJ; X-ray; 3.26 A; A=1-1049.
DR PDB; 4ZLL; X-ray; 3.36 A; A=1-1049.
DR PDB; 4ZLN; X-ray; 3.56 A; A=1-1049.
DR PDB; 5EN5; X-ray; 2.30 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENO; X-ray; 2.20 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENP; X-ray; 1.90 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENQ; X-ray; 1.80 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENR; X-ray; 2.30 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENS; X-ray; 2.80 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5ENT; X-ray; 2.50 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 5JMN; X-ray; 2.50 A; A/B/C=1-1049.
DR PDB; 5NC5; X-ray; 3.20 A; A/B/C=1-1049.
DR PDB; 5NG5; EM; 6.50 A; J/K/L=1-1049.
DR PDB; 5O66; EM; 5.90 A; J/K/L=1-1049.
DR PDB; 5V5S; EM; 6.50 A; J/K/L=1-1049.
DR PDB; 5YIL; X-ray; 3.00 A; A/B/C=1-1049.
DR PDB; 6BAJ; EM; 3.20 A; A/B/C=1-1049.
DR PDB; 6CSX; EM; 3.00 A; A/B/C=1-1049.
DR PDB; 6Q4N; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 6Q4O; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 6Q4P; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 6SGR; EM; 3.17 A; A/B/C=1-1049.
DR PDB; 6SGS; EM; 3.20 A; A/B/C=1-1049.
DR PDB; 6SGT; EM; 3.46 A; A/B/C=1-1049.
DR PDB; 6SGU; EM; 3.27 A; A/B/C=1-1049.
DR PDB; 6ZO5; X-ray; 2.50 A; A/B/C=1-1049.
DR PDB; 6ZO6; X-ray; 2.35 A; A/B/C=1-1049.
DR PDB; 6ZO7; X-ray; 2.85 A; A/B/C=1-1049.
DR PDB; 6ZO8; X-ray; 2.50 A; A/B/C=1-1049.
DR PDB; 6ZO9; X-ray; 2.70 A; A/B/C=1-1049.
DR PDB; 6ZOA; X-ray; 3.05 A; A/B/C=1-1049.
DR PDB; 6ZOB; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 6ZOC; X-ray; 2.89 A; A/B/C=1-1049.
DR PDB; 6ZOD; X-ray; 2.85 A; A/B/C=1-1049.
DR PDB; 6ZOE; X-ray; 2.85 A; A=1-1049.
DR PDB; 6ZOF; X-ray; 3.30 A; A/B/C=1-1049.
DR PDB; 6ZOG; X-ray; 2.75 A; A/B/C=1-1049.
DR PDB; 6ZOH; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 7B8R; X-ray; 2.10 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 7B8S; X-ray; 2.30 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 7B8T; X-ray; 2.70 A; A/B/C=39-329, A/B/C=561-869.
DR PDB; 7OUK; X-ray; 2.60 A; A/B/C=1-1049.
DR PDB; 7OUL; X-ray; 2.80 A; A/B/C=1-1049.
DR PDB; 7OUM; X-ray; 2.45 A; A/B/C=1-1049.
DR PDBsum; 1IWG; -.
DR PDBsum; 1OY6; -.
DR PDBsum; 1OY8; -.
DR PDBsum; 1OY9; -.
DR PDBsum; 1OYD; -.
DR PDBsum; 1OYE; -.
DR PDBsum; 1T9T; -.
DR PDBsum; 1T9U; -.
DR PDBsum; 1T9V; -.
DR PDBsum; 1T9W; -.
DR PDBsum; 1T9X; -.
DR PDBsum; 1T9Y; -.
DR PDBsum; 2DHH; -.
DR PDBsum; 2DR6; -.
DR PDBsum; 2DRD; -.
DR PDBsum; 2GIF; -.
DR PDBsum; 2HQC; -.
DR PDBsum; 2HQD; -.
DR PDBsum; 2HQF; -.
DR PDBsum; 2HQG; -.
DR PDBsum; 2HRT; -.
DR PDBsum; 2I6W; -.
DR PDBsum; 2J8S; -.
DR PDBsum; 2RDD; -.
DR PDBsum; 2W1B; -.
DR PDBsum; 3AOA; -.
DR PDBsum; 3AOB; -.
DR PDBsum; 3AOC; -.
DR PDBsum; 3AOD; -.
DR PDBsum; 3D9B; -.
DR PDBsum; 3NOC; -.
DR PDBsum; 3NOG; -.
DR PDBsum; 3W9H; -.
DR PDBsum; 4C48; -.
DR PDBsum; 4CDI; -.
DR PDBsum; 4DX5; -.
DR PDBsum; 4DX6; -.
DR PDBsum; 4DX7; -.
DR PDBsum; 4K7Q; -.
DR PDBsum; 4U8V; -.
DR PDBsum; 4U8Y; -.
DR PDBsum; 4U95; -.
DR PDBsum; 4U96; -.
DR PDBsum; 4ZIT; -.
DR PDBsum; 4ZIV; -.
DR PDBsum; 4ZIW; -.
DR PDBsum; 4ZJL; -.
DR PDBsum; 4ZJO; -.
DR PDBsum; 4ZJQ; -.
DR PDBsum; 4ZLJ; -.
DR PDBsum; 4ZLL; -.
DR PDBsum; 4ZLN; -.
DR PDBsum; 5EN5; -.
DR PDBsum; 5ENO; -.
DR PDBsum; 5ENP; -.
DR PDBsum; 5ENQ; -.
DR PDBsum; 5ENR; -.
DR PDBsum; 5ENS; -.
DR PDBsum; 5ENT; -.
DR PDBsum; 5JMN; -.
DR PDBsum; 5NC5; -.
DR PDBsum; 5NG5; -.
DR PDBsum; 5O66; -.
DR PDBsum; 5V5S; -.
DR PDBsum; 5YIL; -.
DR PDBsum; 6BAJ; -.
DR PDBsum; 6CSX; -.
DR PDBsum; 6Q4N; -.
DR PDBsum; 6Q4O; -.
DR PDBsum; 6Q4P; -.
DR PDBsum; 6SGR; -.
DR PDBsum; 6SGS; -.
DR PDBsum; 6SGT; -.
DR PDBsum; 6SGU; -.
DR PDBsum; 6ZO5; -.
DR PDBsum; 6ZO6; -.
DR PDBsum; 6ZO7; -.
DR PDBsum; 6ZO8; -.
DR PDBsum; 6ZO9; -.
DR PDBsum; 6ZOA; -.
DR PDBsum; 6ZOB; -.
DR PDBsum; 6ZOC; -.
DR PDBsum; 6ZOD; -.
DR PDBsum; 6ZOE; -.
DR PDBsum; 6ZOF; -.
DR PDBsum; 6ZOG; -.
DR PDBsum; 6ZOH; -.
DR PDBsum; 7B8R; -.
DR PDBsum; 7B8S; -.
DR PDBsum; 7B8T; -.
DR PDBsum; 7OUK; -.
DR PDBsum; 7OUL; -.
DR PDBsum; 7OUM; -.
DR AlphaFoldDB; P31224; -.
DR PCDDB; P31224; -.
DR SMR; P31224; -.
DR BioGRID; 4259859; 386.
DR ComplexPortal; CPX-4263; AcrAB-TolC multidrug efflux transport complex.
DR DIP; DIP-9049N; -.
DR IntAct; P31224; 9.
DR MINT; P31224; -.
DR STRING; 511145.b0462; -.
DR ChEMBL; CHEMBL1681614; -.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugBank; DB04209; Dequalinium.
DR DrugBank; DB03825; Rhodamine 6G.
DR TCDB; 2.A.6.2.2; the resistance-nodulation-cell division (rnd) superfamily.
DR jPOST; P31224; -.
DR PaxDb; P31224; -.
DR PRIDE; P31224; -.
DR EnsemblBacteria; AAC73564; AAC73564; b0462.
DR EnsemblBacteria; BAE76241; BAE76241; BAE76241.
DR GeneID; 66671236; -.
DR GeneID; 945108; -.
DR KEGG; ecj:JW0451; -.
DR KEGG; eco:b0462; -.
DR PATRIC; fig|1411691.4.peg.1814; -.
DR EchoBASE; EB1655; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_0_0_6; -.
DR InParanoid; P31224; -.
DR OMA; LMYMSSS; -.
DR PhylomeDB; P31224; -.
DR BioCyc; EcoCyc:ACRB-MON; -.
DR BioCyc; MetaCyc:ACRB-MON; -.
DR EvolutionaryTrace; P31224; -.
DR PRO; PR:P31224; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IDA:ComplexPortal.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004764; HAE1.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00915; 2A0602; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1049
FT /note="Multidrug efflux pump subunit AcrB"
FT /id="PRO_0000161811"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 10..28
FT /note="Helical; Name=1"
FT TOPO_DOM 29..336
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 337..356
FT /note="Helical; Name=2"
FT TOPO_DOM 357..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 366..385
FT /note="Helical; Name=3"
FT TOPO_DOM 386..391
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 392..413
FT /note="Helical; Name=4"
FT TOPO_DOM 414..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 439..457
FT /note="Helical; Name=5"
FT TOPO_DOM 458..465
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 466..490
FT /note="Helical; Name=6"
FT TOPO_DOM 491..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 539..555
FT /note="Helical; Name=7"
FT TOPO_DOM 556..871
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 872..888
FT /note="Helical; Name=8"
FT TOPO_DOM 889..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 899..918
FT /note="Helical; Name=9"
FT TOPO_DOM 919..924
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 925..943
FT /note="Helical; Name=10"
FT TOPO_DOM 944..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 973..992
FT /note="Helical; Name=11"
FT TOPO_DOM 993..998
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 999..1018
FT /note="Helical; Name=12"
FT TOPO_DOM 1019..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT MUTAGEN 526
FT /note="H->Y: Partially restores chloramphenicol resistance
FT to an AcrZ G30R mutant."
FT /evidence="ECO:0000269|PubMed:23010927"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 9..29
FT /evidence="ECO:0007829|PDB:4DX5"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2GIF"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2DR6"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3W9H"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:5ENQ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1T9X"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:7OUM"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2DHH"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2DHH"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 330..359
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 362..385
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 392..423
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 427..453
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 461..496
FT /evidence="ECO:0007829|PDB:4DX5"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:2GIF"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6Q4P"
FT HELIX 512..536
FT /evidence="ECO:0007829|PDB:4DX5"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:3NOG"
FT HELIX 540..558
FT /evidence="ECO:0007829|PDB:4DX5"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:2DR6"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:6SGR"
FT HELIX 584..599
FT /evidence="ECO:0007829|PDB:5ENQ"
FT TURN 600..605
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 606..616
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 619..631
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:6ZO6"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6BAJ"
FT STRAND 679..686
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 692..707
FT /evidence="ECO:0007829|PDB:5ENQ"
FT TURN 710..712
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 713..720
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 724..731
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 733..739
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 743..755
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 757..764
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 767..775
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 777..779
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 783..788
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:3NOC"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 804..812
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 822..831
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:3NOC"
FT HELIX 837..848
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 855..859
FT /evidence="ECO:0007829|PDB:5ENQ"
FT HELIX 861..863
FT /evidence="ECO:0007829|PDB:5ENQ"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:4DX5"
FT TURN 869..871
FT /evidence="ECO:0007829|PDB:1T9W"
FT HELIX 873..892
FT /evidence="ECO:0007829|PDB:4DX5"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:5YIL"
FT HELIX 898..902
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 905..919
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 925..954
FT /evidence="ECO:0007829|PDB:4DX5"
FT TURN 955..957
FT /evidence="ECO:0007829|PDB:4C48"
FT HELIX 960..985
FT /evidence="ECO:0007829|PDB:4DX5"
FT HELIX 987..990
FT /evidence="ECO:0007829|PDB:4DX5"
FT STRAND 994..996
FT /evidence="ECO:0007829|PDB:2J8S"
FT HELIX 997..1032
FT /evidence="ECO:0007829|PDB:4DX5"
FT TURN 1033..1035
FT /evidence="ECO:0007829|PDB:4K7Q"
FT STRAND 1036..1038
FT /evidence="ECO:0007829|PDB:2GIF"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:2J8S"
SQ SEQUENCE 1049 AA; 113574 MW; 19670E3C4CC29055 CRC64;
MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP GADAKTVQDT
VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA DIAQVQVQNK LQLAMPLLPQ
EVQQQGVSVE KSSSSFLMVV GVINTDGTMT QEDISDYVAA NMKDAISRTS GVGDVQLFGS
QYAMRIWMNP NELNKFQLTP VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL
TSTEEFGKIL LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL
DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL VFLVMYLFLQ
NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM
AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS AVFVPMAFFG GSTGAIYRQF SITIVSAMAL
SVLVALILTP ALCATMLKPI AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR
YLVLYLIIVV GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT
KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR ATRAFSQIKD
AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN QLLAEAAKHP DMLTSVRPNG
LEDTPQFKID IDQEKAQALG VSINDINTTL GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR
MLPDDIGDWY VRAADGQMVP FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA
MELMEQLASK LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS
VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK DLMDKEGKGL
IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ NAVGTGVMGG MVTATVLAIF
FVPVFFVVVR RRFSRKNEDI EHSHTVDHH
