ID ACRE_ECOLI Reviewed; 385 AA.
AC P24180; Q2M8V0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Multidrug export protein AcrE;
DE AltName: Full=Acriflavine resistance protein E;
DE AltName: Full=Protein EnvC;
DE Flags: Precursor;
GN Name=acrE; Synonyms=envC; OrderedLocusNames=b3265, JW3233;
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 acrEF operon from Escherichia coli.";
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1720861; DOI=10.1007/bf00290673;
RA Klein J.R., Henrich B., Plapp R.;
RT "Molecular analysis and nucleotide sequence of the envCD operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 230:230-240(1991).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RC STRAIN=K12;
RA Klein J.R., Henrich B., Plapp R.;
RT "Molecular cloning of the envC gene of Escherichia coli.";
RL Curr. Microbiol. 21:341-347(1990).
RN [6]
RP PROTEIN SEQUENCE OF 291-299, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11274125; DOI=10.1128/jb.183.8.2646-2653.2001;
RA Kobayashi K., Tsukagoshi N., Aono R.;
RT "Suppression of hypersensitivity of Escherichia coli acrB mutant to organic
RT solvents by integrational activation of the acrEF operon with the IS1 or
RT IS2 element.";
RL J. Bacteriol. 183:2646-2653(2001).
RN [7]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=10518736; DOI=10.1111/j.1574-6968.1999.tb08748.x;
RA Kawamura-Sato K., Shibayama K., Horii T., Iimuma Y., Arakawa Y., Ohta M.;
RT "Role of multiple efflux pumps in Escherichia coli in indole expulsion.";
RL FEMS Microbiol. Lett. 179:345-352(1999).
RN [8]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
CC -!- FUNCTION: Part of the tripartite efflux system AcrEF-TolC. Involved in
CC the efflux of indole and organic solvents.
CC {ECO:0000269|PubMed:10518736, ECO:0000269|PubMed:11274125}.
CC -!- SUBUNIT: Part of the tripartite efflux system AcrEF-TolC, which is
CC composed of an inner membrane transporter, AcrF, a periplasmic membrane
CC fusion protein, AcrE, and an outer membrane component, TolC. The
CC complex forms a large protein conduit and can translocate molecules
CC across both the inner and outer membranes (Probable).
CC {ECO:0000305|PubMed:11274125}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:11274125}; Lipid-anchor
CC {ECO:0000305|PubMed:11274125}.
CC -!- INDUCTION: Induced by LeuO, part of the acrEF operon.
CC {ECO:0000269|PubMed:19429622}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; M96848; AAA02931.1; -; Unassigned_DNA.
DR EMBL; X57948; CAA41016.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58069.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76297.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77306.1; -; Genomic_DNA.
DR PIR; C65119; C65119.
DR RefSeq; NP_417731.1; NC_000913.3.
DR RefSeq; WP_000160334.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P24180; -.
DR SMR; P24180; -.
DR BioGRID; 4261953; 367.
DR ComplexPortal; CPX-4265; AcrEF-TolC multidrug efflux transport complex.
DR STRING; 511145.b3265; -.
DR PaxDb; 511145-b3265; -.
DR EnsemblBacteria; AAC76297; AAC76297; b3265.
DR GeneID; 75206113; -.
DR GeneID; 947706; -.
DR KEGG; ecj:JW3233; -.
DR KEGG; eco:b3265; -.
DR PATRIC; fig|1411691.4.peg.3463; -.
DR EchoBASE; EB0262; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_018816_2_1_6; -.
DR InParanoid; P24180; -.
DR OMA; LDPIHAD; -.
DR OrthoDB; 9800613at2; -.
DR PhylomeDB; P24180; -.
DR BioCyc; EcoCyc:EG10266-MONOMER; -.
DR BioCyc; MetaCyc:EG10266-MONOMER; -.
DR PRO; PR:P24180; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; NAS:ComplexPortal.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; NAS:ComplexPortal.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:EcoliWiki.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; EXP:ComplexPortal.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR PANTHER; PTHR30158:SF21; MULTIDRUG EXPORT PROTEIN ACRE; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..385
FT /note="Multidrug export protein AcrE"
FT /id="PRO_0000018688"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 191..212
FT /note="GALVTNGQTTELATVQQLDPIY -> ALLSLMGKRLNWRLSSSSILST (in
FT Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="SR -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41318 MW; EDBF82C853CF42A9 CRC64;
MTKHARFFLL PSFILISAAL IAGCNDKGEE KAHVGEPQVT VHIVKTAPLE VKTELPGRTN
AYRIAEVRPQ VSGIVLNRNF TEGSDVQAGQ SLYQIDPATY QANYDSAKGE LAKSEAAAAI
AHLTVKRYVP LVGTKYISQQ EYDQAIADAR QADAAVIAAK ATVESARINL AYTKVTAPIS
GRIGKSTVTE GALVTNGQTT ELATVQQLDP IYVDVTQSSN DFMRLKQSVE QGNLHKENAT
SNVELVMENG QTYPLKGTLQ FSDVTVDEST GSITLRAVFP NPQHTLLPGM FVRARIDEGV
QPDAILIPQQ GVSRTPRGDA TVLIVNDKSQ VEARPVVASQ AIGDKWLISE GLKSGDQVIV
SGLQKARPGE QVKATTDTPA DTASK
//
