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ACRE_ECOLI
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   03-AUG-2022, entry version 152.
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; 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 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; P24180; -.
DR   PRIDE; P24180; -.
DR   EnsemblBacteria; AAC76297; AAC76297; b3265.
DR   EnsemblBacteria; BAE77306; BAE77306; BAE77306.
DR   GeneID; 66672841; -.
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; NELFPGM; -.
DR   PhylomeDB; P24180; -.
DR   BioCyc; EcoCyc:EG10266-MON; -.
DR   BioCyc; MetaCyc:EG10266-MON; -.
DR   PRO; PR:P24180; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:EcoliWiki.
DR   GO; GO:0098567; C:periplasmic side of plasma membrane; IC: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; IC:ComplexPortal.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR01730; RND_mfp; 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
 
 
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