ACRF_ECOLI
ID ACRF_ECOLI Reviewed; 1034 AA.
AC P24181; Q2M8U9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Multidrug export protein AcrF;
DE AltName: Full=Acriflavine resistance protein F;
DE AltName: Full=Protein EnvD;
GN Name=acrF; Synonyms=envD; OrderedLocusNames=b3266, JW3234;
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., Nilles M.L., 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 PRELIMINARY 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 SEQUENCE REVISION.
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 [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 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 [7]
RP 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 [8]
RP SUBCELLULAR LOCATION.
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 [9]
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 {ECO:0000269|PubMed:11274125,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11274125, ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Induced by LeuO, part of the acrEF operon.
CC {ECO:0000269|PubMed:19429622}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; M96848; AAA02932.1; -; Unassigned_DNA.
DR EMBL; X57948; CAA41017.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58070.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76298.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77307.1; -; Genomic_DNA.
DR PIR; D65119; D65119.
DR RefSeq; NP_417732.1; NC_000913.3.
DR RefSeq; WP_001273238.1; NZ_SSZK01000072.1.
DR AlphaFoldDB; P24181; -.
DR SMR; P24181; -.
DR BioGRID; 4262457; 311.
DR ComplexPortal; CPX-4265; AcrEF-TolC multidrug efflux transport complex.
DR DIP; DIP-9052N; -.
DR IntAct; P24181; 2.
DR STRING; 511145.b3266; -.
DR TCDB; 2.A.6.2.1; the resistance-nodulation-cell division (rnd) superfamily.
DR jPOST; P24181; -.
DR PaxDb; P24181; -.
DR PRIDE; P24181; -.
DR EnsemblBacteria; AAC76298; AAC76298; b3266.
DR EnsemblBacteria; BAE77307; BAE77307; BAE77307.
DR GeneID; 947768; -.
DR KEGG; ecj:JW3234; -.
DR KEGG; eco:b3266; -.
DR PATRIC; fig|1411691.4.peg.3462; -.
DR EchoBASE; EB0263; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_1_1_6; -.
DR InParanoid; P24181; -.
DR OMA; QYESFII; -.
DR PhylomeDB; P24181; -.
DR BioCyc; EcoCyc:ACRF-MON; -.
DR BioCyc; MetaCyc:ACRF-MON; -.
DR PRO; PR:P24181; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC: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 Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1034
FT /note="Multidrug export protein AcrF"
FT /id="PRO_0000161813"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 29..339
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..359
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..385
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 386..391
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 392..413
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 414..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..460
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 461..473
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 474..496
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 497..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 538..556
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 557..871
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 872..891
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 892..897
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 898..917
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 918..923
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 924..945
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 946..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 974..992
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250"
FT TOPO_DOM 993..1005
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1006..1028
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1029..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1034 AA; 111454 MW; B676E07AE5BD17B1 CRC64;
MANFFIRRPI FAWVLAIILM MAGALAILQL PVAQYPTIAP PAVSVSANYP GADAQTVQDT
VTQVIEQNMN GIDNLMYMSS TSDSAGSVTI TLTFQSGTDP DIAQVQVQNK LQLATPLLPQ
EVQQQGISVE KSSSSYLMVA GFVSDNPGTT QDDISDYVAS NVKDTLSRLN GVGDVQLFGA
QYAMRIWLDA DLLNKYKLTP VDVINQLKVQ NDQIAAGQLG GTPALPGQQL NASIIAQTRF
KNPEEFGKVT LRVNSDGSVV RLKDVARVEL GGENYNVIAR INGKPAAGLG IKLATGANAL
DTAKAIKAKL AELQPFFPQG MKVLYPYDTT PFVQLSIHEV VKTLFEAIML VFLVMYLFLQ
NMRATLIPTI AVPVVLLGTF AILAAFGYSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM
MEDKLPPKEA TEKSMSQIQG ALVGIAMVLS AVFIPMAFFG GSTGAIYRQF SITIVSAMAL
SVLVALILTP ALCATLLKPV SAEHHENKGG FFGWFNTTFD HSVNHYTNSV GKILGSTGRY
LLIYALIVAG MVVLFLRLPS SFLPEEDQGV FLTMIQLPAG ATQERTQKVL DQVTDYYLKN
EKANVESVFT VNGFSFSGQA QNAGMAFVSL KPWEERNGDE NSAEAVIHRA KMELGKIRDG
FVIPFNMPAI VELGTATGFD FELIDQAGLG HDALTQARNQ LLGMAAQHPA SLVSVRPNGL
EDTAQFKLEV DQEKAQALGV SLSDINQTIS TALGGTYVND FIDRGRVKKL YVQADAKFRM
LPEDVDKLYV RSANGEMVPF SAFTTSHWVY GSPRLERYNG LPSMEIQGEA APGTSSGDAM
ALMENLASKL PAGIGYDWTG MSYQERLSGN QAPALVAISF VVVFLCLAAL YESWSIPVSV
MLVVPLGIVG VLLAATLFNQ KNDVYFMVGL LTTIGLSAKN AILIVEFAKD LMEKEGKGVV
EATLMAVRMR LRPILMTSLA FILGVLPLAI SNGAGSGAQN AVGIGVMGGM VSATLLAIFF
VPVFFVVIRR CFKG
