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 27-MAR-2024, entry version 204. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7B5P; EM; 3.20 A; A/B/C=2-1049. 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; 7O3L; X-ray; 3.53 A; A/B/C/D/E/F=1-1049. DR PDB; 7O3M; X-ray; 3.55 A; A/B/C/D/E/F=1-1049. DR PDB; 7O3N; X-ray; 3.56 A; A/B/C/D/E/F=1-1049. 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 PDB; 7RR6; EM; 3.10 A; A/B/C=1-1049. DR PDB; 7RR7; EM; 3.05 A; A/B/C=1-1049. DR PDB; 7RR8; EM; 3.51 A; A/B/C=1-1049. DR PDB; 8PX7; X-ray; 3.40 A; A=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; 7B5P; -. DR PDBsum; 7B8R; -. DR PDBsum; 7B8S; -. DR PDBsum; 7B8T; -. DR PDBsum; 7O3L; -. DR PDBsum; 7O3M; -. DR PDBsum; 7O3N; -. DR PDBsum; 7OUK; -. DR PDBsum; 7OUL; -. DR PDBsum; 7OUM; -. DR PDBsum; 7RR6; -. DR PDBsum; 7RR7; -. DR PDBsum; 7RR8; -. DR PDBsum; 8PX7; -. DR AlphaFoldDB; P31224; -. DR EMDB; EMD-10182; -. DR EMDB; EMD-10183; -. DR EMDB; EMD-10184; -. DR EMDB; EMD-10185; -. DR EMDB; EMD-24653; -. DR EMDB; EMD-24654; -. DR EMDB; EMD-24655; -. DR EMDB; EMD-25400; -. DR EMDB; EMD-2714; -. DR EMDB; EMD-3636; -. DR EMDB; EMD-7074; -. DR EMDB; EMD-7609; -. DR EMDB; EMD-8636; -. DR EMDB; EMD-8640; -. 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; 511145-b0462; -. DR EnsemblBacteria; AAC73564; AAC73564; b0462. DR GeneID; 75202887; -. 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; GVFYEQF; -. DR OrthoDB; 9757904at2; -. DR PhylomeDB; P31224; -. DR BioCyc; EcoCyc:ACRB-MONOMER; -. DR BioCyc; MetaCyc:ACRB-MONOMER; -. DR EvolutionaryTrace; P31224; -. DR PRO; PR:P31224; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:1990281; C:efflux pump complex; 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; NAS: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; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2. DR Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 1. DR Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR027463; AcrB_DN_DC_subdom. DR InterPro; IPR001036; Acrflvin-R. DR InterPro; IPR004764; MdtF-like. DR NCBIfam; TIGR00915; 2A0602; 1. DR PANTHER; PTHR32063; -; 1. DR PANTHER; PTHR32063:SF13; MULTIDRUG EFFLUX PUMP SUBUNIT ACRB-RELATED; 1. DR Pfam; PF00873; ACR_tran; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. 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 AcrZG30R 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 //