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Multidrug export protein AcrF (Acriflavine resistance protein F) (Protein EnvD)

 ACRF_ECOLI              Reviewed;        1034 AA.
P24181; Q2M8U9;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 2.
25-OCT-2017, entry version 143.
RecName: Full=Multidrug export protein AcrF;
AltName: Full=Acriflavine resistance protein F;
AltName: Full=Protein EnvD;
Name=acrF; Synonyms=envD; OrderedLocusNames=b3266, JW3234;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Xu J., Nilles M.L., Bertrand K.P.;
"Nucleotide sequence of the acrEF operon from Escherichia coli.";
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[2]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1720861; DOI=10.1007/BF00290673;
Klein J.R., Henrich B., Plapp R.;
"Molecular analysis and nucleotide sequence of the envCD operon of
Escherichia coli.";
Mol. Gen. Genet. 230:230-240(1991).
[3]
SEQUENCE REVISION.
PubMed=8407802; DOI=10.1128/jb.175.19.6299-6313.1993;
Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
"Molecular cloning and characterization of acrA and acrE genes of
Escherichia coli.";
J. Bacteriol. 175:6299-6313(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION.
STRAIN=K12;
PubMed=10518736; DOI=10.1111/j.1574-6968.1999.tb08748.x;
Kawamura-Sato K., Shibayama K., Horii T., Iimuma Y., Arakawa Y.,
Ohta M.;
"Role of multiple efflux pumps in Escherichia coli in indole
expulsion.";
FEMS Microbiol. Lett. 179:345-352(1999).
[7]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11274125; DOI=10.1128/JB.183.8.2646-2653.2001;
Kobayashi K., Tsukagoshi N., Aono R.;
"Suppression of hypersensitivity of Escherichia coli acrB mutant to
organic solvents by integrational activation of the acrEF operon with
the IS1 or IS2 element.";
J. Bacteriol. 183:2646-2653(2001).
[8]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[9]
OPERON STRUCTURE, AND INDUCTION.
STRAIN=K12 / BW25113;
PubMed=19429622; DOI=10.1128/JB.00108-09;
Shimada T., Yamamoto K., Ishihama A.;
"Involvement of the leucine response transcription factor LeuO in
regulation of the genes for sulfa drug efflux.";
J. Bacteriol. 191:4562-4571(2009).
-!- FUNCTION: Part of the tripartite efflux system AcrEF-TolC.
Involved in the efflux of indole and organic solvents.
{ECO:0000269|PubMed:10518736, ECO:0000269|PubMed:11274125}.
-!- SUBUNIT: Part of the tripartite efflux system AcrEF-TolC, which is
composed of an inner membrane transporter, AcrF, a periplasmic
membrane fusion protein, AcrE, and an outer membrane component,
TolC. The complex forms a large protein conduit and can
translocate molecules across both the inner and outer membranes
(Probable). {ECO:0000305|PubMed:11274125}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:11274125, ECO:0000269|PubMed:15919996}; Multi-
pass membrane protein {ECO:0000269|PubMed:11274125,
ECO:0000269|PubMed:15919996}.
-!- INDUCTION: Induced by LeuO, part of the acrEF operon.
{ECO:0000269|PubMed:19429622}.
-!- SIMILARITY: Belongs to the resistance-nodulation-cell division
(RND) (TC 2.A.6) family. {ECO:0000305}.
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EMBL; M96848; AAA02932.1; -; Unassigned_DNA.
EMBL; X57948; CAA41017.1; -; Genomic_DNA.
EMBL; U18997; AAA58070.1; -; Genomic_DNA.
EMBL; U00096; AAC76298.1; -; Genomic_DNA.
EMBL; AP009048; BAE77307.1; -; Genomic_DNA.
PIR; D65119; D65119.
RefSeq; NP_417732.1; NC_000913.3.
RefSeq; WP_001273238.1; NZ_LN832404.1.
ProteinModelPortal; P24181; -.
SMR; P24181; -.
BioGrid; 4262457; 308.
DIP; DIP-9052N; -.
IntAct; P24181; 2.
MINT; MINT-1267966; -.
STRING; 316385.ECDH10B_3441; -.
TCDB; 2.A.6.2.1; the resistance-nodulation-cell division (rnd) superfamily.
PaxDb; P24181; -.
PRIDE; P24181; -.
EnsemblBacteria; AAC76298; AAC76298; b3266.
EnsemblBacteria; BAE77307; BAE77307; BAE77307.
GeneID; 947768; -.
KEGG; ecj:JW3234; -.
KEGG; eco:b3266; -.
PATRIC; fig|1411691.4.peg.3462; -.
EchoBASE; EB0263; -.
EcoGene; EG10267; acrF.
eggNOG; ENOG4105BZS; Bacteria.
eggNOG; COG0841; LUCA.
HOGENOM; HOG000158129; -.
InParanoid; P24181; -.
KO; K18142; -.
PhylomeDB; P24181; -.
BioCyc; EcoCyc:ACRF-MONOMER; -.
PRO; PR:P24181; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
Gene3D; 3.30.2090.10; -; 1.
InterPro; IPR027463; AcrB_DN_DC_subdom.
InterPro; IPR001036; Acrflvin-R.
InterPro; IPR004764; HAE1.
PANTHER; PTHR32063; PTHR32063; 1.
Pfam; PF00873; ACR_tran; 1.
PRINTS; PR00702; ACRIFLAVINRP.
SUPFAM; SSF82714; SSF82714; 2.
TIGRFAMs; TIGR00915; 2A0602; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1034 Multidrug export protein AcrF.
/FTId=PRO_0000161813.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000250}.
TRANSMEM 10 28 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 29 339 Periplasmic. {ECO:0000250}.
TRANSMEM 340 359 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 360 365 Cytoplasmic. {ECO:0000250}.
TRANSMEM 366 385 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 386 391 Periplasmic. {ECO:0000250}.
TRANSMEM 392 413 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 414 441 Cytoplasmic. {ECO:0000250}.
TRANSMEM 442 460 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 461 473 Periplasmic. {ECO:0000250}.
TRANSMEM 474 496 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 497 537 Cytoplasmic. {ECO:0000250}.
TRANSMEM 538 556 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 557 871 Periplasmic. {ECO:0000250}.
TRANSMEM 872 891 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 892 897 Cytoplasmic. {ECO:0000250}.
TRANSMEM 898 917 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 918 923 Periplasmic. {ECO:0000250}.
TRANSMEM 924 945 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 946 973 Cytoplasmic. {ECO:0000250}.
TRANSMEM 974 992 Helical; Name=11. {ECO:0000250}.
TOPO_DOM 993 1005 Periplasmic. {ECO:0000250}.
TRANSMEM 1006 1028 Helical; Name=12. {ECO:0000250}.
TOPO_DOM 1029 1034 Cytoplasmic. {ECO:0000250}.
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


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